https://www.cazypedia.org/api.php?action=feedcontributions&user=Amanda+Photenhauer&feedformat=atomCAZypedia - User contributions [en-ca]2024-03-29T11:28:22ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=17256Carbohydrate Binding Module Family 742023-05-23T00:39:35Z<p>Amanda Photenhauer: </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:Amanda Photenhauer|Amanda Photenhauer]]<br />
* [[Responsible Curator]]: [[User:Nicole Koropatkin|Nicole Koropatkin]]<br />
----<br />
CBM74 is a starch-binding CBM that was originally characterized as a discreet domain of a raw starch degrading amylase from the bacterium, ''Microbacterium aurum''. ''Microbacterium aurum'' was isolated from the waste sludge of a potato starch processing facility so it may be no surprise that ''Ma''CBM74 binds raw potato, corn, and wheat starches. CBM74 doesn't fit the paradigm of CBMs in that it consists of 300-350 amino acids as opposed to the canonical 100-150 amino acids. The molecular basis for binding remains unknown.<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type<cite> Valk2016 </cite>.<br />
<br />
== Structural Features ==<br />
<br />
CBM74 is predicted to be a discrete domain of approximately 300 amino acids. No CBM74 three dimensional structure has yet been determined. The most similar predicted structure is that of CBM9 from of a xylanase from <i>Thermotoga maritima</i> MSB8<cite> Valk2016 </cite>. Trp71 of CBM9 is conserved among all identified CBM74 domains and may be involved in starch binding<cite>Janecek2019</cite>.<br />
<br />
== Functionalities == <br />
<br />
* '''Functional role of CBM:''' Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy <cite> Valk2016 </cite>. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed. <br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above. So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Sas6 from the bacterium ''Ruminococcus bromii'' has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a GH13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.<br />
:3. FNIII (FN3) or Bacterial Ig-like2 (BIG2)<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
#Candussio1990 pmid=1696201<br />
#Candussio1991 pmid=1714389<br />
#Janecek2019 pmid=31536775<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=17255Carbohydrate Binding Module Family 742023-05-23T00:38:21Z<p>Amanda Photenhauer: </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:Amanda Photenhauer|Amanda Photenhauer]]<br />
* [[Responsible Curator]]: [[User:Nicole Koropatkin|Nicole Koropatkin]]<br />
----<br />
CBM74 is a starch-binding CBM that was originally characterized as a discreet domain of a raw starch degrading amylase from the bacterium, ''Microbacterium aurum''. ''Microbacterium aurum'' was isolated from the waste sludge of a potato starch processing facility so it may be no surprise that ''Ma''CBM74 binds raw potato, corn, and wheat starches. CBM74 doesn't fit the paradigm of CBMs in that it consists of 300-350 amino acids as opposed to the canonical 100-150 amino acids. The molecular basis for binding remains unknown.<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type<cite> Valk2016 </cite>.<br />
<br />
== Structural Features ==<br />
<br />
CBM74 is predicted to be a discrete domain of approximately 300 amino acids. No CBM74 three dimensional structure has yet been determined. The most similar predicted structure is that of CBM9 from of a xylanase from <i>Thermotoga maritima</i> MSB8<cite> Valk2016 </cite>. Trp71 of CBM9 is conserved among all identified CBM74 domains and may be involved in starch binding<cite>Janecek2019</cite>.<br />
<br />
== Functionalities == <br />
<br />
* '''Functional role of CBM:''' Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy <cite> Valk2016 </cite>. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed. <br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above. So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.<br />
:3. FNIII or Bacterial Ig-like2<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
#Candussio1990 pmid=1696201<br />
#Candussio1991 pmid=1714389<br />
#Janecek2019 pmid=31536775<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=16383Carbohydrate Binding Module Family 742021-11-10T01:36:50Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<br />
----<br />
CBM74 is a starch-binding CBM that was originally characterized as a discreet domain of a raw starch degrading amylase from the bacterium, ''Microbacterium aurum''. ''Microbacterium aurum'' was isolated from the waste sludge of a potato starch processing facility so it may be no surprise that ''Ma''CBM74 binds raw potato, corn, and wheat starches. CBM74 doesn't fit the paradigm of CBMs in that it consists of 300-350 amino acids as opposed to the canonical 100-150 amino acids. The molecular basis for binding remains unknown.<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type<cite> Valk2016 </cite>.<br />
<br />
== Structural Features ==<br />
<br />
CBM74 is predicted to be a discrete domain of approximately 300 amino acids. No CBM74 three dimensional structure has yet been determined. The most similar predicted structure is that of CBM9 from of a xylanase from <i>Thermotoga maritima</i> MSB8<cite> Valk2016 </cite>. Trp71 of CBM9 is conserved among all identified CBM74 domains and may be involved in starch binding<cite>Janecek2019</cite>.<br />
<br />
== Functionalities == <br />
<br />
* '''Functional role of CBM:''' Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy <cite> Valk2016 </cite>. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed. <br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above. So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.<br />
:3. FNIII or Bacterial Ig-like2<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
#Candussio1990 pmid=1696201<br />
#Candussio1991 pmid=1714389<br />
#Janecek2019 pmid=31536775<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=16382Carbohydrate Binding Module Family 742021-11-10T01:36:21Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<br />
----<br />
CBM74 is a starch-binding CBM that was originally characterized as a discreet domain of a raw starch degrading amylase from the bacterium, ''Microbacterium aurum''. ''Microbacterium aurum'' was isolated from the waste sludge of a potato starch processing facility so it may be no surprise that ''Ma''CBM74 binds raw potato, corn, and wheat starches. CBM74 doesn't fit the paradigm of CBMs in that it consists of 300-350 amino acids as opposed to the canonical 100-150 amino acids. The molecular basis remains unknown.<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type<cite> Valk2016 </cite>.<br />
<br />
== Structural Features ==<br />
<br />
CBM74 is predicted to be a discrete domain of approximately 300 amino acids. No CBM74 three dimensional structure has yet been determined. The most similar predicted structure is that of CBM9 from of a xylanase from <i>Thermotoga maritima</i> MSB8<cite> Valk2016 </cite>. Trp71 of CBM9 is conserved among all identified CBM74 domains and may be involved in starch binding<cite>Janecek2019</cite>.<br />
<br />
== Functionalities == <br />
<br />
* '''Functional role of CBM:''' Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy <cite> Valk2016 </cite>. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed. <br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above. So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.<br />
:3. FNIII or Bacterial Ig-like2<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
#Candussio1990 pmid=1696201<br />
#Candussio1991 pmid=1714389<br />
#Janecek2019 pmid=31536775<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=16146Carbohydrate Binding Module Family 742020-12-07T05:44:02Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type<cite> Valk2016 </cite>.<br />
<br />
== Structural Features ==<br />
<br />
CBM74 is predicted to be a discrete domain of approximately 300 amino acids. No CBM74 three dimensional structure has yet been determined and has not been modeled with high confidence by protein structure prediction tools. The most similar predicted structure is that of CBM9 from of a xylanase from <i>Thermotoga maritima</i> MSB8<cite> Valk2016 </cite>. Trp71 of CBM9 is conserved among all identified CBM74 domains and may be involved in starch binding<cite>Janecek2019</cite>.<br />
<br />
== Functionalities == <br />
<br />
* '''Functional role of CBM:''' Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy <cite> Valk2016 </cite>. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed. <br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above. So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.<br />
:3. FNIII or Bacterial Ig-like2<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
#Candussio1990 pmid=1696201<br />
#Candussio1991 pmid=1714389<br />
#Janecek2019 pmid=31536775<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=16145Carbohydrate Binding Module Family 742020-12-07T05:42:33Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
<br />
CBM74 is predicted to be a discrete domain of approximately 300 amino acids. No CBM74 three dimensional structure has yet been determined and has not been modeled with high confidence by protein structure prediction tools. The most similar predicted structure is that of CBM9 from of a xylanase from <i>Thermotoga maritima</i> MSB8<cite> Valk2016 </cite>. Trp71 of CBM9 is conserved among all identified CBM74 domains and may be involved in starch binding<cite>Janecek2019</cite>.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy <cite> Valk2016 </cite>. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed. <br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above. So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.<br />
:3. FNIII or Bacterial Ig-like2<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
#Candussio1990 pmid=1696201<br />
#Candussio1991 pmid=1714389<br />
#Janecek2019 pmid=31536775<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=15923Carbohydrate Binding Module Family 742020-10-23T19:17:41Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Aside from starch binding, additional roles of CBM74 in raw starch degradation remain unclear. The deletion of the CBM74 domain of MaAmyA resulted in smaller, but not fewer, pores on starch granules as shown by Scanning Electron Microscopy <cite> Valk2016 </cite>. This suggests that CBM74 may contribute to local polysaccharide chain disruption or may keep the enzyme in close proximity to the areas that have already been hydrolyzed. <br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above.So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.<br />
:3. FNIII or Bacterial Ig-like2<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
#Candussio1990 pmid=1696201<br />
#Candussio1991 pmid=1714389<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14626Carbohydrate Binding Module Family 742020-03-29T23:52:19Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |http://www.cazy.org/CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above.So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.<br />
:3. FNIII or Bacterial Ig-like2<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
#Candussio1990 pmid=1696201<br />
#Candussio1991 pmid=1714389<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14625Carbohydrate Binding Module Family 742020-03-29T23:44:07Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |http://www.cazy.org/CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above.So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes an adjacent CBM25 or CBM26 domain.<br />
:3. FNIII or Bacterial Ig-like2<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14624Carbohydrate Binding Module Family 742020-03-29T23:43:27Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |http://www.cazy.org/CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' <br />
:1. Glycoside Hydrolase: CBM74 is a starch-binding CBM and as such is associated only with GH13 domains. The GH13 subfamilies are listed in the table above.So far, two CBM74-containing proteins have been characterized.<br />
<br />
::In some cases CBM74 is not appended to any GH13 domain. For example, Doc6 from the bacterium Ruminococcus bromii is has a CBM26, a CBM74, and a dockerin domain for cohesin-dockerin protein assembly, possibly with a Gh13-containing protein.<br />
:2. CBM25 or CBM26: In every CBM74 domain listed in the CAZy database encodes a CBM25 or CBM26 adjacent.<br />
:3. FNIII or Bacterial Ig-like2<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14623Carbohydrate Binding Module Family 742020-03-29T23:27:56Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |http://www.cazy.org/CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=User:Amanda_Photenhauer&diff=14232User:Amanda Photenhauer2019-08-16T03:37:24Z<p>Amanda Photenhauer: </p>
<hr />
<div>[[Image:Photenhauer.jpeg|200px|right]]<br />
'''PhD student in the Koropatkin lab at the University of Michigan'''<br />
<br />
Amanda is a PhD student in the lab of ^^^Nicole_Koropatkin^^^ studying resistant starch degradation mechanisms by human gut symbionts.<br />
<br />
<br />
<biblio><br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Photenhauer,Amanda]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14231Carbohydrate Binding Module Family 742019-08-16T03:26:25Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH27.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14230Carbohydrate Binding Module Family 742019-08-16T03:21:41Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
<br />
|'''Associated GH Families''' <br />
|GH13_28<br>GH13_19<br>GH13_32<br>none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH27.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion in which unbound protein is measured following incubation with and centrifugation of starch granules. <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14229Carbohydrate Binding Module Family 742019-08-16T03:13:19Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''Carbohydrate Binding Module Family 74'''<br />
|-<br />
|'''Carbohydrate Specificity''' <br />
|Starch<br />
<br />
|-<br />
<br />
|'''Associated GH Families''' <br />
|GH13_28<br />
<br />
GH13_19<br />
<br />
GH13_32<br />
<br />
none<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH27.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion in which unbound protein is measured following incubation with and centrifugation of starch granules. <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14228Carbohydrate Binding Module Family 742019-08-16T02:49:01Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion in which unbound protein is measured following incubation with and centrifugation of starch granules. <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14227Carbohydrate Binding Module Family 742019-08-16T02:44:40Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
<br />
The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from wheat, waxy corn, and potato as shown by adsorption depletion in which unbound protein is measured following incubation with and centrifugation of starch granules. <cite> Valk2016 </cite><br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14083Carbohydrate Binding Module Family 742019-07-30T16:17:08Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.<br />
<br />
''Note: Here is an example of how to insert references in the text, together with the "biblio" section below:'' Please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. CBMs, in particular, have been extensively reviewed <cite>Boraston2004 Hashimoto2006 Shoseyov2006 Guillen2010</cite>.<br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from <i>Microbacterium aurum</i><cite>Valk2016</cite>.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14082Carbohydrate Binding Module Family 742019-07-30T16:05:06Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.<br />
<br />
''Note: Here is an example of how to insert references in the text, together with the "biblio" section below:'' Please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. CBMs, in particular, have been extensively reviewed <cite>Boraston2004 Hashimoto2006 Shoseyov2006 Guillen2010</cite>.<br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:Insert archetype here, possibly including ''very brief'' synopsis.<br />
;First Structural Characterization<br />
:No structure has yet been determined for any CBM74 family member.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_74&diff=14081Carbohydrate Binding Module Family 742019-07-30T16:02:53Z<p>Amanda Photenhauer: </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]]: ^^^Amanda Photenhauer^^^<br />
* [[Responsible Curator]]: ^^^Nicole Koropatkin^^^<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" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM74.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.<br />
<br />
''Note: Here is an example of how to insert references in the text, together with the "biblio" section below:'' Please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. CBMs, in particular, have been extensively reviewed <cite>Boraston2004 Hashimoto2006 Shoseyov2006 Guillen2010</cite>.<br />
<br />
== Structural Features ==<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities == <br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:Insert archetype here, possibly including ''very brief'' synopsis.<br />
;First Structural Characterization<br />
:Insert archetype here, possibly including ''very brief'' synopsis.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Valk2016 pmid=27101946<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM074]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=User:Amanda_Photenhauer&diff=14072User:Amanda Photenhauer2019-07-23T01:57:34Z<p>Amanda Photenhauer: </p>
<hr />
<div>[[Image:Photenhauer.jpeg|200px|right]]<br />
'''PhD student in the Koropatkin lab at the University of Michigan'''<br />
<br />
Amanda is a PhD student in the lab of [[User:Nicole_Koropatkin]] studying resistant starch degradation mechanisms by human gut symbionts.<br />
<br />
* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.<br />
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.<br />
<br />
<br />
''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Gilbert2008 pmid=18430603<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Photenhauer,Amanda]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=User:Amanda_Photenhauer&diff=14071User:Amanda Photenhauer2019-07-23T01:56:44Z<p>Amanda Photenhauer: </p>
<hr />
<div>[[Image:Photenhauer.jpeg|200px|right]]<br />
'''PhD student in the Koropatkin lab at the University of Michigan'''<br />
<br />
Amanda is a PhD student in the lab of Nicole Koropatkin studying resistant starch degradation mechanisms by human gut symbionts.<br />
<br />
* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.<br />
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.<br />
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<br />
''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Gilbert2008 pmid=18430603<br />
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</biblio><br />
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<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Photenhauer,Amanda]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=User:Amanda_Photenhauer&diff=14070User:Amanda Photenhauer2019-07-23T01:56:06Z<p>Amanda Photenhauer: </p>
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<div>[[Image:Photenhauer.jpeg|200px|right]]<br />
'''PhD student in the Koropatkin lab at the University of Michigan'''<br />
<br />
Amanda is a PhD student in the lab of Nicole Koropatkin studying resistant starch degradation mechanisms by human gut symbionts.<br />
<br />
* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.<br />
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.<br />
* Please upload a picture of yourself using the "Upload file" link in the Toolbox section of the left menu, and then replace the Image filename with your own.<br />
<br />
''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Gilbert2008 pmid=18430603<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Photenhauer,Amanda]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=User:Amanda_Photenhauer&diff=14069User:Amanda Photenhauer2019-07-23T01:51:38Z<p>Amanda Photenhauer: </p>
<hr />
<div>[[Image:Photenhauer.jpeg|200px|right]]<br />
'''This is an empty template to help you get started with composing your User page.'''<br />
<br />
You should begin by opening this page for editing by clicking on the Edit tab above. Your biography goes in this area of the page.<br />
<br />
* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.<br />
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.<br />
* Please upload a picture of yourself using the "Upload file" link in the Toolbox section of the left menu, and then replace the Image filename with your own.<br />
<br />
''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Gilbert2008 pmid=18430603<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Photenhauer,Amanda]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=User:Amanda_Photenhauer&diff=14068User:Amanda Photenhauer2019-07-23T01:48:24Z<p>Amanda Photenhauer: </p>
<hr />
<div>[[Image:Photenhauer.jpg|200px|right]]<br />
'''This is an empty template to help you get started with composing your User page.'''<br />
<br />
You should begin by opening this page for editing by clicking on the Edit tab above. Your biography goes in this area of the page.<br />
<br />
* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.<br />
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.<br />
* Please upload a picture of yourself using the "Upload file" link in the Toolbox section of the left menu, and then replace the Image filename with your own.<br />
<br />
''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Gilbert2008 pmid=18430603<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Photenhauer,Amanda]]</div>Amanda Photenhauerhttps://www.cazypedia.org/index.php?title=File:Photenhauer.jpeg&diff=14067File:Photenhauer.jpeg2019-07-23T01:31:03Z<p>Amanda Photenhauer: </p>
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<div></div>Amanda Photenhauer