https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Wei+PengCAZypedia - User contributions [en-ca]2026-04-28T16:59:26ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19683Glycosyltransferase Family 1382025-12-17T17:33:19Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1250px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left, image from <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures (image from''' <cite>Peng2024</cite>''').''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold (Fig. 1A) <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB (Fig. 1A) <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Kim_Orth&diff=19682User:Kim Orth2025-12-10T19:08:39Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Kim-Orth.png|150px|right]]<br />
Kim Orth is a Professor of Molecular Biology and Biochemistry at UT Southwestern Medical Center and is an Investigator for the Howard Hughes Medical Institute. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.<br />
<br />
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.<br />
<br />
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Kim contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Kim_Orth&diff=19681User:Kim Orth2025-12-09T05:13:36Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Kim-Orth.png|150px|right]]<br />
Kim Orth is a Professor of Molecular Biology and Biochemistry at UT Southwestern Medical Center and is an Investigator for the Howard Hughes Medical Institute. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.<br />
<br />
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.<br />
<br />
The marine bacterium ''Vibrio parahaemolyticus'' is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two ''V. parahaemolyticus'' type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more.<br />
<br />
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Kim contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Kim_Orth&diff=19680User:Kim Orth2025-12-09T05:11:43Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Kim-Orth.png|150px|right]]<br />
Kim Orth is a '''Professor of Molecular Biology and Biochemistry at UT Southwestern Medical Center''' and is an '''Investigator for the Howard Hughes Medical Institute'''. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.<br />
<br />
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.<br />
<br />
The marine bacterium ''Vibrio parahaemolyticus'' is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two ''V. parahaemolyticus'' type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more.<br />
<br />
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Kim contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Kim_Orth&diff=19679User:Kim Orth2025-12-09T05:10:50Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Kim-Orth.png|150px|right]]<br />
Kim Orth is a Professor of '''Molecular Biology and Biochemistry''' at '''UT Southwestern Medical Center''' and is an Investigator for the '''Howard Hughes Medical Institute'''. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.<br />
<br />
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.<br />
<br />
The marine bacterium ''Vibrio parahaemolyticus'' is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two ''V. parahaemolyticus'' type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more.<br />
<br />
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Kim contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19678Glycosyltransferase Family 1382025-12-08T20:28:47Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1250px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left, image from <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures (image from''' <cite>Peng2024</cite>''').''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19677Glycosyltransferase Family 1382025-12-08T20:26:44Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1250px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left, image from <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures (image from <cite>Peng2024</cite>''').''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19676Glycosyltransferase Family 1382025-12-08T20:25:40Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1250px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left, image from <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures (image from <cite>Peng2024</cite>''')'''.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19675Glycosyltransferase Family 1382025-12-08T20:23:59Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1250px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19674Glycosyltransferase Family 1382025-12-08T20:23:48Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19673Glycosyltransferase Family 1382025-12-08T20:23:31Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1400px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19672Glycosyltransferase Family 1382025-12-08T20:23:14Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1200px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19671Glycosyltransferase Family 1382025-12-08T19:46:10Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Wei_Peng&diff=19670User:Wei Peng2025-12-08T19:44:05Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Wei-Peng.jpeg|150px|right]]<br />
Wei Peng obtained his Ph.D. at Tsinghua University (Beijing, China) with Prof. Yigong Shi and Prof. Nieng Yan. He was trained as a structural biologist using protein crystallography/cryo-EM and other tools to investigate protein functions. As a postdoctoral scholar with Prof. Kim Orth at UT Southwestern Medical Center (Dallas, USA), he has been focusing on host-pathogen interactions. <br />
<br />
Wei and colleagues discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Wei contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Kim_Orth&diff=19669User:Kim Orth2025-12-08T19:43:51Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Kim-Orth.png|150px|right]]<br />
Kim Orth is a Professor of Molecular Biology and Biochemistry and is an Investigator for the Howard Hughes Medical Institute. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.<br />
<br />
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.<br />
<br />
The marine bacterium ''Vibrio parahaemolyticus'' is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two ''V. parahaemolyticus'' type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more.<br />
<br />
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Kim contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Wei_Peng&diff=19668User:Wei Peng2025-12-08T19:43:36Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Wei-Peng.jpeg|200px|right]]<br />
Wei Peng obtained his Ph.D. at Tsinghua University (Beijing, China) with Prof. Yigong Shi and Prof. Nieng Yan. He was trained as a structural biologist using protein crystallography/cryo-EM and other tools to investigate protein functions. As a postdoctoral scholar with Prof. Kim Orth at UT Southwestern Medical Center (Dallas, USA), he has been focusing on host-pathogen interactions. <br />
<br />
Wei and colleagues discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Wei contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Kim_Orth&diff=19667User:Kim Orth2025-12-08T19:43:13Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Kim-Orth.png|200px|right]]<br />
Kim Orth is a Professor of Molecular Biology and Biochemistry and is an Investigator for the Howard Hughes Medical Institute. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.<br />
<br />
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.<br />
<br />
The marine bacterium ''Vibrio parahaemolyticus'' is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two ''V. parahaemolyticus'' type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more.<br />
<br />
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Kim contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Kim_Orth&diff=19666User:Kim Orth2025-12-08T19:41:50Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Kim-Orth.png|200px|right]]<br />
Kim Orth is a Professor of Molecular Biology and Biochemistry and is an Investigator for the Howard Hughes Medical Institute. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.<br />
<br />
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.<br />
<br />
The marine bacterium Vibrio parahaemolyticus is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two V. parahaemolyticus type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more.<br />
<br />
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Kim contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Kim_Orth&diff=19665User:Kim Orth2025-12-08T19:41:03Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Kim-Orth.png|150px|right]]<br />
Kim Orth is a Professor of Molecular Biology and Biochemistry and is an Investigator for the Howard Hughes Medical Institute. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.<br />
<br />
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.<br />
<br />
The marine bacterium Vibrio parahaemolyticus is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two V. parahaemolyticus type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more.<br />
<br />
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Kim contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=File:Kim-Orth.png&diff=19664File:Kim-Orth.png2025-12-08T19:40:25Z<p>Wei Peng: </p>
<hr />
<div></div>Wei Penghttps://www.cazypedia.org/index.php?title=User:Kim_Orth&diff=19663User:Kim Orth2025-12-08T19:39:30Z<p>Wei Peng: </p>
<hr />
<div>[[Image:Kim-Orth.jpeg|150px|right]]<br />
Kim Orth is a Professor of Molecular Biology and Biochemistry and is an Investigator for the Howard Hughes Medical Institute. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.<br />
<br />
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.<br />
<br />
The marine bacterium Vibrio parahaemolyticus is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two V. parahaemolyticus type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more.<br />
<br />
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]].<br />
<br />
Kim contributed to studies on:<br />
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite><br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Peng,Wei]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19662Glycosyltransferase Family 1382025-12-05T16:46:24Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19661Glycosyltransferase Family 1382025-12-05T16:45:39Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19660Glycosyltransferase Family 1382025-12-05T16:44:06Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19659Glycosyltransferase Family 1382025-12-05T16:43:42Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Family members ==<br />
<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19658Glycosyltransferase Family 1382025-12-05T16:42:48Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Family members ==<br />
<br />
AvrB is the only well-studied member so far in the GT138 family.<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19657Glycosyltransferase Family 1382025-12-05T16:37:43Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19656Glycosyltransferase Family 1382025-12-05T16:36:14Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19655Glycosyltransferase Family 1382025-12-05T16:34:24Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19654Glycosyltransferase Family 1382025-12-05T16:34:03Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite> , different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19653Glycosyltransferase Family 1382025-12-05T16:33:50Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite> , different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> . <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19652Glycosyltransferase Family 1382025-12-05T16:33:33Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite> , different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19651Glycosyltransferase Family 1382025-12-05T16:32:59Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to rhamnosylate the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19650Glycosyltransferase Family 1382025-12-05T16:32:38Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19649Glycosyltransferase Family 1382025-12-05T16:32:06Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the rhamnosylation reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19648Glycosyltransferase Family 1382025-12-05T16:31:16Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19647Glycosyltransferase Family 1382025-12-05T16:31:05Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). <br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19646Glycosyltransferase Family 1382025-12-05T16:30:11Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19645Glycosyltransferase Family 1382025-12-05T16:28:45Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Family features ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19644Glycosyltransferase Family 1382025-12-05T16:28:31Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Family features ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19643Glycosyltransferase Family 1382025-12-05T16:28:03Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Family features ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19642Glycosyltransferase Family 1382025-12-05T16:27:37Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Kinetics and Mechanism ==<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19641Glycosyltransferase Family 1382025-12-05T16:21:24Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19640Glycosyltransferase Family 1382025-12-05T04:45:02Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''', a Fido protein (Fig. 1A) <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures <cite>Peng2024</cite>.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19639Glycosyltransferase Family 1382025-12-05T04:43:51Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''', a Fido protein (Fig. 1A) <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19638Glycosyltransferase Family 1382025-12-05T04:42:54Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''', a Fido protein (Fig. 1A) <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2). The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2).<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19637Glycosyltransferase Family 1382025-12-05T04:35:45Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''', a Fido protein (Fig. 1A) <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>). In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2). <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2). The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2).<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19636Glycosyltransferase Family 1382025-12-05T04:32:49Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''', a Fido protein (Fig. 1A) <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>). In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2). <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2). The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2).<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19635Glycosyltransferase Family 1382025-12-05T04:28:09Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''', a Fido protein (Fig. 1A) <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>). In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2). <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2). The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2).<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available for revealing the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Penghttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19634Glycosyltransferase Family 1382025-12-05T04:26:12Z<p>Wei Peng: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' '''(or dTDP-rhamnose ''in vitro'')''' '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
== Kinetics and Mechanism ==<br />
AvrB contains a '''Fido''' domain <cite>Lee2004, Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite> (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>). In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2). <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures.''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2). The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2).<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB <cite>Lee2004</cite>. A few AvrB structures are available for revealing the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Wei Peng