CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 173

2023-06-21T12:57:06Z

Clelton Santos:

{{UnderConstruction}}
* [[Author]]s: [[User:Clelton Santos|Clelton Aparecido dos Santos]] and [[User:Gabriela Persinoti|Gabriela Felix Persinoti]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH173'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining (inferred)
|-
|'''Active site residues'''
|known (inferred)
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH173.html
|}
</div>


== Substrate specificities ==
The GH173 family comprises so far members with β-galactosidase activity <cite>Cabral2022</cite>. The founding member of the GH173 family named herein as CapGH173 ([https://www.ncbi.nlm.nih.gov/nuccore/2205462651 PBMDCECB_44807]), was identified in a metagenome-assembled genome (''Bacteroidales bacterium'' MAG42) recovered from capybara gut microbiota, which potentially represents a novel genus from the UBA932 family. The enzyme CapGH173 was found in a Polysaccharide Utilization Loci (PUL) that includes enzymes from the families GH2 and GH78, remaining yet unclear the target carbohydrate. GH173 members often exhibit a modular architecture including a GH36 domain. Substrate kinetics characterization of CapGH173 was demonstrated on synthetic substrate ''p''-nitrophenyl-β-D-galactopyranoside (pNP-β-D-Gal). Phylogenetic analysis showed that this family belongs to the GH-A clan, being remotely related to the families GH30 and GH5 <cite>Cabral2022</cite>.

== Kinetics and Mechanism ==
GH173 members are inferred to be retaining enzymes <cite>Cabral2022</cite>.

== Catalytic Residues ==
The residues E305 and E207 was inferred to correspond to the nucleophile and acid/base, respectively, based on the structural analysis of AlphaFold models <cite>Cabral2022</cite>.

== Three-dimensional structures ==
Protein modeling and threading performed using AlphaFold and PDBsum, respectively, suggest that CapGH173 consists of an (α/β)<sub>8</sub>-barrel structure, which is an archetypal scaffold of the clan GH-A. According to structural predictions, CapGH173 exhibits a two-domain architecture including an appended β-sandwich domain, which is a similar structural organization found in the GH30 family. Except for the residues defining the clan GH-A, sequence alignment with GH5 and GH30 members revealed very low sequence conservation, below the criterium for significant similarity detection (using an e-value < 0.05), demonstrating that although the domains in the tertiary structure can be similar, the sequences between these families are remarkably diverse <cite>Cabral2022</cite>.  

== Family Firsts ==
;First stereochemistry determination: CapGH173 is inferred to operate by a retaining mechanism.
;First catalytic nucleophile identification: E305 (inferred).
;First general acid/base residue identification: E207 (inferred).
;First 3-D structure: Currently no experimental structure is available for GH173 members.

== References ==
<biblio>

#Cabral2022 pmid=35110564
</biblio>

[[Category:Glycoside Hydrolase Families|GH173]]

User:Clelton Santos

2023-06-19T19:10:18Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at the University of Cambridge and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory ([https://lnbr.cnpem.br/en/ LNBR]) from the National Center for Research in Energy and Materials ([https://cnpem.br/en/ CNPEM]) in Campinas, Sao Paulo, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families [[Glycoside_Hydrolase_Family_1|GH1]] <cite>Santos2016; Santos2019</cite> [[Glycoside_Hydrolase_Family_54|GH54]] <cite>Motta2021</cite> [[Glycoside_Hydrolase_Family_173|GH173]] <cite>Cabral2022</cite> [[Carbohydrate_Binding_Module_Family_89|CBM89]] <cite>Cabral2022</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Motta2021 pmid=34040092

#Cabral2022 pmid=35110564
</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T19:09:42Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at the University of Cambridge and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory ([https://lnbr.cnpem.br/en/ LNBR]) from the National Center for Research in Energy and Materials (CNPEM) in Campinas, Sao Paulo, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families [[Glycoside_Hydrolase_Family_1|GH1]] <cite>Santos2016; Santos2019</cite> [[Glycoside_Hydrolase_Family_54|GH54]] <cite>Motta2021</cite> [[Glycoside_Hydrolase_Family_173|GH173]] <cite>Cabral2022</cite> [[Carbohydrate_Binding_Module_Family_89|CBM89]] <cite>Cabral2022</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Motta2021 pmid=34040092

#Cabral2022 pmid=35110564
</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T19:08:07Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at the University of Cambridge and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory ([https://lnbr.cnpem.br/en/ LNBR]) from the National Center for Research in Energy and Materials in Campinas, Sao Paulo, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families [[Glycoside_Hydrolase_Family_1|GH1]] <cite>Santos2016; Santos2019</cite> [[Glycoside_Hydrolase_Family_54|GH54]] <cite>Motta2021</cite> [[Glycoside_Hydrolase_Family_173|GH173]] <cite>Cabral2022</cite> [[Carbohydrate_Binding_Module_Family_89|CBM89]] <cite>Cabral2022</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Motta2021 pmid=34040092

#Cabral2022 pmid=35110564
</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T19:04:27Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at the University of Cambridge and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families [[Glycoside_Hydrolase_Family_1|GH1]] <cite>Santos2016; Santos2019</cite> [[Glycoside_Hydrolase_Family_54|GH54]] <cite>Motta2021</cite> [[Glycoside_Hydrolase_Family_173|GH173]] <cite>Cabral2022</cite> [[Carbohydrate_Binding_Module_Family_89|CBM89]] <cite>Cabral2022</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Motta2021 pmid=34040092

#Cabral2022 pmid=35110564
</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T18:57:48Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families [[Glycoside_Hydrolase_Family_1|GH1]] <cite>Santos2016; Santos2019</cite> [[Glycoside_Hydrolase_Family_54|GH54]] <cite>Motta2021</cite> [[Glycoside_Hydrolase_Family_173|GH173]] <cite>Cabral2022</cite> [[Carbohydrate_Binding_Module_Family_89|CBM89]] <cite>Cabral2022</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Motta2021 pmid=34040092

#Cabral2022 pmid=35110564
</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T18:56:28Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families [[Glycoside_Hydrolase_Family_1|GH1]] <cite>Santos2016; Santos2019</cite> [[Glycoside_Hydrolase_Family_54|GH54]] <cite>Motta2021</cite> [[Glycoside_Hydrolase_Family_173|GH173]] <cite>Cabral2022</cite> [[Carbohydrate_Binding_Module_Family_89|CBM89]] <cite>Cabral2022</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Motta2021 pmid=34040092

#Cabral2022 pmid=35110564
</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T18:53:44Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families [[Glycoside_Hydrolase_Family_1|GH1]] <cite>Santos2016; Santos2019</cite> GH54 <cite>Motta2021</cite> GH173 <cite>Cabral2022</cite> CBM89 <cite>Cabral2022</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Motta2021 pmid=34040092

#Cabral2022 pmid=35110564
</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T18:51:43Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families [[https://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_1|GH1]] <cite>Santos2016; Santos2019</cite> GH54 <cite>Motta2021</cite> GH173 <cite>Cabral2022</cite> CBM89 <cite>Cabral2022</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Motta2021 pmid=34040092

#Cabral2022 pmid=35110564
</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T18:48:15Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families GH1 <cite>Santos2016; Santos2019</cite> GH54 <cite>Motta2021</cite> GH173 <cite>Cabral2022</cite> CBM89 <cite>Cabral2022</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Motta2021 pmid=34040092

#Cabral2022 pmid=35110564
</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T18:43:24Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families GH1 <cite>Santos2016; Santos2019</cite> GH54 [ref] GH173 [ref] CBM89 [ref] <cite>Gilbert2008</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Santos2019 pmid=30894609

#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T18:40:41Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families GH1 <cite>Santos2016</cite> GH54 [ref] GH173 [ref] CBM89 [ref] <cite>Gilbert2008</cite>.

----

<biblio>

#Santos2016 pmid=27006690

#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T18:40:01Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families GH1 <cite>Santos2016</cite> GH54 [ref] GH173 [ref] CBM89 [ref] <cite>Gilbert2008</cite>.

----

<biblio>

#Santos2016 pmcid=4802607

#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T16:22:39Z

Clelton Santos:

[[Image:Clelton-200px.png|200px|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families GH1 [ref] GH54 [ref] GH173 [ref] CBM89 [ref] <cite>Gilbert2008</cite>.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T16:22:01Z

Clelton Santos:

[[Image:Clelton-200px.png|thumb|200px|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families GH1 [ref] GH54 [ref] GH173 [ref] CBM89 [ref] <cite>Gilbert2008</cite>.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

File:Clelton-200px.png

2023-06-19T14:44:22Z

Clelton Santos: Profile photo

== Summary ==
Profile photo

User:Clelton Santos

2023-06-19T14:40:48Z

Clelton Santos:

[[File:Clelton200px|250 × 250 (81 KB)px|thumb|right]]

'''This is an empty template to help you get started with composing your User page.'''

Dr Clelton Santos is a Biologist and holds an MS and Ph.D. in Genetics and Molecular Biology. After Postdoc jobs at Cambridge University and the National University of Ireland Galway, He becomes a Research Scientist at the Brazilian Biorenewables National Laboratory National from the Center for Research in Energy and Materials in Campinas, Brazil. His research interests combine structural enzymology and protein engineering for protein discovery and biotechnology application purposes.

He has contributed to structural and functional studies of CAZymes from families GH1 [ref] GH54 [ref] GH173 [ref] CBM89 [ref] <cite>Gilbert2008</cite>.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T14:33:17Z

Clelton Santos:

[[File:Clelton200px|250 × 250 (81 KB)px|thumb|right]]

'''This is an empty template to help you get started with composing your User page.'''

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.

* 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.
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.
* 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.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T14:32:52Z

Clelton Santos:

[[File:Clelton200px|250 × 250 (81 KB)px|thumb|right|clelton200px]]

'''This is an empty template to help you get started with composing your User page.'''

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.

* 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.
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.
* 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.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

File:Clelton200px.jpeg

2023-06-19T14:31:34Z

Clelton Santos: Profile photo

== Summary ==
Profile photo

User:Clelton Santos

2023-06-19T14:24:34Z

Clelton Santos:

[[File:Clelton|250 × 250 (81 KB)px|thumb|right|clelton]]

'''This is an empty template to help you get started with composing your User page.'''

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.

* 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.
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.
* 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.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

User:Clelton Santos

2023-06-19T14:19:43Z

Clelton Santos:

[[Image:filen[[File:Clelton.jpg|right]]

'''This is an empty template to help you get started with composing your User page.'''

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.

* 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.
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.
* 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.

''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Santos,Clelton]]

File:Clelton.jpg

2023-06-19T14:18:59Z

Clelton Santos:

Profile photo.

Glycoside Hydrolase Family 173

2023-06-16T13:36:44Z

Clelton Santos:

{{UnderConstruction}}
* [[Author]]s: [[User:Clelton Santos|Clelton Aparecido dos Santos]] and [[User:Gabriela Persinoti|Gabriela Felix Persinoti]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH173'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining (inferred)
|-
|'''Active site residues'''
|known (inferred)
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH173.html
|}
</div>


== Substrate specificities ==
The GH173 family comprises members with β-galactosidase activity <cite>Cabral2022</cite>. The founding member of the GH173 family named herein as CapGH173 ([https://www.ncbi.nlm.nih.gov/nuccore/2205462651 PBMDCECB_44807]), was identified in a novel metagenome-assembled genome (MAG) recovered from the ''Bacteroidales bacterium'' MAG42, a novel genus among the Uncultivated Bacteria and Archaea family (UBA932). CapGH173 was found in a Polysaccharide Utilization Loci (PUL) that includes enzymes from families GH2 and GH78; however, a multidomain protein organization was also predicted among GH173 members, having an additional GH36 domain. Biochemical characterization of CapGH173 showed it is active on ''p''-nitrophenyl-β-D-galactopyranoside (pNP-β-D-Gal) and kinetic parameters were determined from substrate saturation curves. Phylogenetic analysis showed that CapGH173 is remotely related to GH-A CAZy families, with GH30 and GH5 being the closest ones <cite>Cabral2022</cite>.

== Kinetics and Mechanism ==
Family GH173 members are retaining enzymes (inferred <cite>Cabral2022</cite>).

== Catalytic Residues ==
The residues E305 and E207 correspond to the nucleophile and acid/base, respectively (inferred by structural superposition) <cite>Cabral2022</cite>.

== Three-dimensional structures ==
Protein modeling and threading performed using AlphaFold and PDBsum, respectively, revealed that CapGH173 consists of an (α/β)<sub>8</sub>-barrel structure, which is an archetypal scaffold of the clan GH-A. According to structural predictions, CapGH173 exhibits a two-domain architecture including an appended β-sandwich domain, which is a similar structural organization found in the GH30 family. Except for the residues defining the clan GH-A, sequence alignment with GH5 and GH30 members revealed a very low sequence conservation below the criterium for significant similarity detection (using an e-value < 0.05), demonstrating that although the domains in the tertiary structure can be similar, the sequences between these families are remarkably diverse <cite>Cabral2022</cite>.  

== Family Firsts ==
;First stereochemistry determination: CpGH173 is shown to have an inferred retaining mechanism.
;First catalytic nucleophile identification: E305 (inferred).
;First general acid/base residue identification: E207 (inferred).
;First 3-D structure: Currently no experimental structure is available for GH173 members.

== References ==
<biblio>

#Cabral2022 pmid=35110564
</biblio>

[[Category:Glycoside Hydrolase Families|GH173]]

Glycoside Hydrolase Family 173

2023-06-16T13:31:41Z

Clelton Santos:

{{UnderConstruction}}
* [[Author]]s: [[User:Clelton Santos|Clelton Aparecido dos Santos]] and [[User:Gabriela Persinoti|Gabriela Felix Persinoti]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH173'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining (inferred)
|-
|'''Active site residues'''
|known (inferred)
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH173.html
|}
</div>


== Substrate specificities ==
The GH173 family comprises members with β-galactosidase activity <cite>Cabral2022</cite>. The founding member of the GH173 family named herein as CapGH173 ([PBMDCECB_44807]), was identified in a novel metagenome-assembled genome (MAG) recovered from the ''Bacteroidales bacterium'' MAG42, a novel genus among the Uncultivated Bacteria and Archaea family (UBA932). CapGH173 was found in a Polysaccharide Utilization Loci (PUL) that includes enzymes from families GH2 and GH78; however, a multidomain protein organization was also predicted among GH173 members, having an additional GH36 domain. Biochemical characterization of CapGH173 showed it is active on ''p''-nitrophenyl-β-D-galactopyranoside (pNP-β-D-Gal) and kinetic parameters were determined from substrate saturation curves. Phylogenetic analysis showed that CapGH173 is remotely related to GH-A CAZy families, with GH30 and GH5 being the closest ones <cite>Cabral2022</cite>.

== Kinetics and Mechanism ==
Family GH173 members are retaining enzymes (inferred <cite>Cabral2022</cite>).

== Catalytic Residues ==
The residues E305 and E207 correspond to the nucleophile and acid/base, respectively (inferred by structural superposition) <cite>Cabral2022</cite>.

== Three-dimensional structures ==
Protein modeling and threading performed using AlphaFold and PDBsum, respectively, revealed that CapGH173 consists of an (α/β)<sub>8</sub>-barrel structure, which is an archetypal scaffold of the clan GH-A. According to structural predictions, CapGH173 exhibits a two-domain architecture including an appended β-sandwich domain, which is a similar structural organization found in the GH30 family. Except for the residues defining the clan GH-A, sequence alignment with GH5 and GH30 members revealed a very low sequence conservation below the criterium for significant similarity detection (using an e-value < 0.05), demonstrating that although the domains in the tertiary structure can be similar, the sequences between these families are remarkably diverse <cite>Cabral2022</cite>.  

== Family Firsts ==
;First stereochemistry determination: CpGH173 is shown to have an inferred retaining mechanism.
;First catalytic nucleophile identification: E305 (inferred).
;First general acid/base residue identification: E207 (inferred).
;First 3-D structure: Currently no experimental structure is available for GH173 members.

== References ==
<biblio>

#Cabral2022 pmid=35110564
</biblio>

[[Category:Glycoside Hydrolase Families|GH173]]

Glycoside Hydrolase Family 173

2023-06-16T13:28:39Z

Clelton Santos:

{{UnderConstruction}}
* [[Author]]s: [[User:Clelton Santos|Clelton Aparecido dos Santos]] and [[User:Gabriela Persinoti|Gabriela Felix Persinoti]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH173'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining (inferred)
|-
|'''Active site residues'''
|known (inferred)
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH173.html
|}
</div>


== Substrate specificities ==
The GH173 family comprises members with β-galactosidase activity <cite>Cabral2022</cite>. The founding member of the GH173 family named herein as CapGH173 [[PBMDCECB_44807]], was identified in a novel metagenome-assembled genome (MAG) recovered from the ''Bacteroidales bacterium'' MAG42, a novel genus among the Uncultivated Bacteria and Archaea family (UBA932). CapGH173 was found in a Polysaccharide Utilization Loci (PUL) that includes enzymes from families GH2 and GH78; however, a multidomain protein organization was also predicted among GH173 members, having an additional GH36 domain. Biochemical characterization of CapGH173 showed it is active on ''p''-nitrophenyl-β-D-galactopyranoside (pNP-β-D-Gal) and kinetic parameters were determined from substrate saturation curves. Phylogenetic analysis showed that CapGH173 is remotely related to GH-A CAZy families, with GH30 and GH5 being the closest ones <cite>Cabral2022</cite>.

== Kinetics and Mechanism ==
Family GH173 members are retaining enzymes (inferred <cite>Cabral2022</cite>).

== Catalytic Residues ==
The residues E305 and E207 correspond to the nucleophile and acid/base, respectively (inferred by structural superposition) <cite>Cabral2022</cite>.

== Three-dimensional structures ==
Protein modeling and threading performed using AlphaFold and PDBsum, respectively, revealed that CapGH173 consists of an (α/β)<sub>8</sub>-barrel structure, which is an archetypal scaffold of the clan GH-A. According to structural predictions, CapGH173 exhibits a two-domain architecture including an appended β-sandwich domain, which is a similar structural organization found in the GH30 family. Except for the residues defining the clan GH-A, sequence alignment with GH5 and GH30 members revealed a very low sequence conservation below the criterium for significant similarity detection (using an e-value < 0.05), demonstrating that although the domains in the tertiary structure can be similar, the sequences between these families are remarkably diverse <cite>Cabral2022</cite>.  

== Family Firsts ==
;First stereochemistry determination: CpGH173 is shown to have an inferred retaining mechanism.
;First catalytic nucleophile identification: E305 (inferred).
;First general acid/base residue identification: E207 (inferred).
;First 3-D structure: Currently no experimental structure is available for GH173 members.

== References ==
<biblio>

#Cabral2022 pmid=35110564
</biblio>

[[Category:Glycoside Hydrolase Families|GH173]]

Glycoside Hydrolase Family 173

2023-06-16T13:25:08Z

Clelton Santos:

{{UnderConstruction}}
* [[Author]]s: [[User:Clelton Santos|Clelton Aparecido dos Santos]] and [[User:Gabriela Persinoti|Gabriela Felix Persinoti]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH173'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining (inferred)
|-
|'''Active site residues'''
|known (inferred)
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH173.html
|}
</div>


== Substrate specificities ==
The GH173 family comprises members with β-galactosidase activity <cite>Cabral2022</cite>. The founding member of the GH173 family named herein as CapGH173 ([[PBMDCECB_44807]]), was identified in a novel metagenome-assembled genome (MAG) recovered from the ''Bacteroidales bacterium'' MAG42, a novel genus among the Uncultivated Bacteria and Archaea family (UBA932). CapGH173 was found in a Polysaccharide Utilization Loci (PUL) that includes enzymes from families GH2 and GH78; however, a multidomain protein organization was also predicted among GH173 members, having an additional GH36 domain. Biochemical characterization of CapGH173 showed it is active on ''p''-nitrophenyl-β-D-galactopyranoside (pNP-β-D-Gal) and kinetic parameters were determined from substrate saturation curves. Phylogenetic analysis showed that CapGH173 is remotely related to GH-A CAZy families, with GH30 and GH5 being the closest ones <cite>Cabral2022</cite>.

== Kinetics and Mechanism ==
Family GH173 members are retaining enzymes (inferred <cite>Cabral2022</cite>).

== Catalytic Residues ==
The residues E305 and E207 correspond to the nucleophile and acid/base, respectively (inferred by structural superposition) <cite>Cabral2022</cite>.

== Three-dimensional structures ==
Protein modeling and threading performed using AlphaFold and PDBsum, respectively, revealed that CapGH173 consists of an (α/β)<sub>8</sub>-barrel structure, which is an archetypal scaffold of the clan GH-A. According to structural predictions, CapGH173 exhibits a two-domain architecture including an appended β-sandwich domain, which is a similar structural organization found in the GH30 family. Except for the residues defining the clan GH-A, sequence alignment with GH5 and GH30 members revealed a very low sequence conservation below the criterium for significant similarity detection (using an e-value < 0.05), demonstrating that although the domains in the tertiary structure can be similar, the sequences between these families are remarkably diverse <cite>Cabral2022</cite>.  

== Family Firsts ==
;First stereochemistry determination: CpGH173 is shown to have an inferred retaining mechanism.
;First catalytic nucleophile identification: E305 (inferred).
;First general acid/base residue identification: E207 (inferred).
;First 3-D structure: Currently no experimental structure is available for GH173 members.

== References ==
<biblio>

#Cabral2022 pmid=35110564
</biblio>

[[Category:Glycoside Hydrolase Families|GH173]]

Glycoside Hydrolase Family 173

2023-06-16T13:16:01Z

Clelton Santos:

{{UnderConstruction}}
* [[Author]]s: [[User:Clelton Santos|Clelton Aparecido dos Santos]] and [[User:Gabriela Persinoti|Gabriela Felix Persinoti]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH173'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining (inferred)
|-
|'''Active site residues'''
|known (inferred)
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH173.html
|}
</div>


== Substrate specificities ==
The GH173 family comprises members with β-galactosidase activity <cite>Cabral2022</cite>. The founding member of the GH173 family named herein as CapGH173 (PBMDCECB_44807), was identified in a novel metagenome-assembled genome (MAG) recovered from the ''Bacteroidales bacterium'' MAG42, a novel genus among the Uncultivated Bacteria and Archaea family (UBA932). CapGH173 was found in a Polysaccharide Utilization Loci (PUL) that includes enzymes from families GH2 and GH78; however, a multidomain protein organization was also predicted among GH173 members, having an additional GH36 domain. Biochemical characterization of CapGH173 showed it is active on ''p''-nitrophenyl-β-D-galactopyranoside (pNP-β-D-Gal) and kinetic parameters were determined from substrate saturation curves. Phylogenetic analysis showed that CapGH173 is remotely related to GH-A CAZy families, with GH30 and GH5 being the closest ones <cite>Cabral2022</cite>.

== Kinetics and Mechanism ==
Family GH173 members are retaining enzymes (inferred <cite>Cabral2022</cite>).

== Catalytic Residues ==
The residues E305 and E207 correspond to the nucleophile and acid/base, respectively (inferred by structural superposition) <cite>Cabral2022</cite>.

== Three-dimensional structures ==
Protein modeling and threading performed using AlphaFold and PDBsum, respectively, revealed that CapGH173 consists of an (α/β)<sub>8</sub>-barrel structure, which is an archetypal scaffold of the clan GH-A. According to structural predictions, CapGH173 exhibits a two-domain architecture including an appended β-sandwich domain, which is a similar structural organization found in the GH30 family. Except for the residues defining the clan GH-A, sequence alignment with GH5 and GH30 members revealed a very low sequence conservation below the criterium for significant similarity detection (using an e-value < 0.05), demonstrating that although the domains in the tertiary structure can be similar, the sequences between these families are remarkably diverse <cite>Cabral2022</cite>.  

== Family Firsts ==
;First stereochemistry determination: CpGH173 is shown to have an inferred retaining mechanism.
;First catalytic nucleophile identification: E305 (inferred).
;First general acid/base residue identification: E207 (inferred).
;First 3-D structure: Currently no experimental structure is available for GH173 members.

== References ==
<biblio>

#Cabral2022 pmid=35110564
</biblio>

[[Category:Glycoside Hydrolase Families|GH173]]

Glycoside Hydrolase Family 173

2023-06-15T18:57:50Z

Clelton Santos:

{{UnderConstruction}}
* [[Author]]s: [[User:Clelton Santos|Clelton Aparecido dos Santos]] and [[User:Gabriela Persinoti|Gabriela Felix Persinoti]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH173'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retainingi (inferred)
|-
|'''Active site residues'''
|known (inferred)
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH173.html
|}
</div>


== Substrate specificities ==
The GH173 family comprises members with β-galactosidase activity <cite>Cabral2022</cite>. The founding member of the GH173 family named herein as CapGH173 (PBMDCECB_44807), was identified in a novel metagenome-assembled genome (MAG) recovered from the Bacteroidales bacterium MAG42, a novel genus among the Uncultivated Bacteria and Archaea family (UBA932). CapGH173 was found in a Polysaccharide Utilization Loci (PUL) that includes enzymes from families GH2 and GH78; however, a multidomain protein organization was also predicted among GH173 members, having an additional GH36 domain. Biochemical characterization of CapGH173 showed it is active on p-nitrophenyl-β-D-galactopyranoside (pNP-β-D-Gal) and kinetic parameters were determined from substrate saturation curves. Phylogenetic analysis showed that CapGH173 is remotely related to GH-A CAZy families, with GH30 and GH5 being the closest ones <cite>Cabral2022</cite>.

== Kinetics and Mechanism ==
Family GH173 members are retaining enzymes (inferred <cite>Cabral2022</cite>).

== Catalytic Residues ==
The residues E305 and E207 correspond to the nucleophile and acid/base, respectively (inferred by structural superposition) <cite>Cabral2022</cite>.

== Three-dimensional structures ==
Protein modeling and threading performed using AlphaFold and PDBsum, respectively, revealed that CapGH173 consists of an (α/β)8-barrel structure, which is an archetypal scaffold of the clan GH-A. According to structural predictions, CapGH173 exhibits a two-domain architecture including an appended β-sandwich domain, which is a similar structural organization found in the GH30 family. Except for the residues defining the clan GH-A, sequence alignment with GH5 and GH30 members revealed a very low sequence conservation below the criterium for significant similarity detection (using an e-value < 0.05), demonstrating that although the domains in the tertiary structure can be similar, the sequences between these families are remarkably diverse <cite>Cabral2022</cite>.  

== Family Firsts ==
;First stereochemistry determination: CpGH173 is shown to have an inferred retaining mechanism.
;First catalytic nucleophile identification: E305 (inferred).
;First general acid/base residue identification: E207 (inferred).
;First 3-D structure: Currently no experimental structure is available for GH173 members.

== References ==
<biblio>

#Cabral2022 pmid=35110564
</biblio>

[[Category:Glycoside Hydrolase Families|GH173]]

Glycoside Hydrolase Family 173

2023-06-15T18:54:41Z

Clelton Santos:

{{UnderConstruction}}
* [[Author]]s: [[User:Clelton Santos|Clelton Aparecido dos Santos]] and [[User:Gabriela Persinoti|Gabriela Felix Persinoti]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH173'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retainingi (inferred)
|-
|'''Active site residues'''
|known (inferred)
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH173.html
|}
</div>


== Substrate specificities ==
The GH173 family comprises members with β-galactosidase activity <cite>Cabral2022</cite>. The founding member of the GH173 family named herein as CapGH173 (PBMDCECB_44807), was identified in a novel metagenome-assembled genome (MAG) recovered from the Bacteroidales bacterium MAG42, a novel genus among the Uncultivated Bacteria and Archaea family (UBA932). CapGH173 was found in a Polysaccharide Utilization Loci (PUL) that includes enzymes from families GH2 and GH78; however, a multidomain protein organization was also predicted among GH173 members, having an additional GH36 domain. Biochemical characterization of CapGH173 showed it is active on p-nitrophenyl-β-D-galactopyranoside (pNP-β-D-Gal) and kinetic parameters were determined from substrate saturation curves. Phylogenetic analysis showed that CapGH173 is remotely related to GH-A CAZy families, with GH30 and GH5 being the closest ones <cite>Cabral2022</cite>.

== Kinetics and Mechanism ==
Content is to be added here.

== Catalytic Residues ==
The residues E305 and E207 correspond to the nucleophile and acid/base, respectively (inferred by structural superposition) <cite>Cabral2022</cite>.

== Three-dimensional structures ==
Protein modeling and threading performed using AlphaFold and PDBsum, respectively, revealed that CapGH173 consists of an (α/β)8-barrel structure, which is an archetypal scaffold of the clan GH-A. According to structural predictions, CapGH173 exhibits a two-domain architecture including an appended β-sandwich domain, which is a similar structural organization found in the GH30 family. Except for the residues defining the clan GH-A, sequence alignment with GH5 and GH30 members revealed a very low sequence conservation below the criterium for significant similarity detection (using an e-value < 0.05), demonstrating that although the domains in the tertiary structure can be similar, the sequences between these families are remarkably diverse <cite>Cabral2022</cite>.  

== Family Firsts ==
;First stereochemistry determination: CpGH173 is shown to have an inferred retaining mechanism.
;First catalytic nucleophile identification: E305 (inferred).
;First general acid/base residue identification: E207 (inferred).
;First 3-D structure: Currently no experimental structure is available for GH173 members.

== References ==
<biblio>

#Cabral2022 pmid=35110564
</biblio>

[[Category:Glycoside Hydrolase Families|GH173]]

Glycoside Hydrolase Family 173

2023-06-15T18:44:54Z

Clelton Santos:

{{UnderConstruction}}
* [[Author]]s: [[User:Clelton Santos|Clelton Aparecido dos Santos]] and [[User:Gabriela Persinoti|Gabriela Felix Persinoti]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH173'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retainingi (inferred)
|-
|'''Active site residues'''
|known (inferred)
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH173.html
|}
</div>


== Substrate specificities ==
The GH173 family comprises members with β-galactosidase activity <cite>Cabral2022</cite>. The founding member of the GH173 family named herein as CapGH173, was identified in a novel metagenome-assembled genome (MAG) recovered from the Bacteroidales bacterium MAG42, a novel genus among the Uncultivated Bacteria and Archaea family (UBA932). CapGH173 was found in a Polysaccharide Utilization Loci (PUL) that includes enzymes from families GH2 and GH78; however, a multidomain protein organization was also predicted among GH173 members, having an additional GH36 domain. Biochemical characterization of CapGH173 showed it is active on p-nitrophenyl-β-D-galactopyranoside (pNP-β-D-Gal) and kinetic parameters were determined from substrate saturation curves. Phylogenetic analysis showed that CapGH173 is remotely related to GH-A CAZy families, with GH30 and GH5 being the closest ones <cite>Cabral2022</cite>.

== Kinetics and Mechanism ==
Content is to be added here.

== Catalytic Residues ==
Content is to be added here.

== Three-dimensional structures ==
Protein modeling and threading performed using AlphaFold and PDBsum, respectively, revealed that CapGH173 consists of an (α/β)8-barrel structure, which is an archetypal scaffold of the clan GH-A. According to structural predictions, CapGH173 exhibits a two-domain architecture including an appended β-sandwich domain, which is a similar structural organization found in the GH30 family. Except for the residues defining the clan GH-A, sequence alignment with GH5 and GH30 members revealed a very low sequence conservation below the criterium for significant similarity detection (using an e-value < 0.05), demonstrating that although the domains in the tertiary structure can be similar, the sequences between these families are remarkably diverse <cite>Cabral2022</cite>.  

== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
;First catalytic nucleophile identification: Content is to be added here.
;First general acid/base residue identification: Content is to be added here.
;First 3-D structure: Content is to be added here.

== References ==
<biblio>

#Cabral2022 pmid=35110564
</biblio>

[[Category:Glycoside Hydrolase Families|GH173]]

Glycoside Hydrolase Family 173

2023-06-15T18:21:11Z

Clelton Santos:

Glycoside Hydrolase Family 173

2023-06-15T18:18:32Z

Clelton Santos:

Glycoside Hydrolase Family 173

2023-06-15T18:17:15Z

Clelton Santos:

Glycoside Hydrolase Family 173

2023-06-15T18:14:32Z

Clelton Santos:

Glycoside Hydrolase Family 173

2023-06-15T18:13:47Z

Clelton Santos: