CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.

Difference between revisions of "Glycosyltransferase Family 138"

From CAZypedia
Jump to navigation Jump to search
Line 31: Line 31:
 
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite> that contains a '''Fido''' domain <cite>Kinch2009</cite> (Fig. 1A). AvrB is different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Therefore, AvrB is a unique Fido protein that functions as a glycosyltransferase. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' (or dTDP-rhamnose ''in vitro'') '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response).  
 
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite> that contains a '''Fido''' domain <cite>Kinch2009</cite> (Fig. 1A). AvrB is different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Therefore, AvrB is a unique Fido protein that functions as a glycosyltransferase. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' (or dTDP-rhamnose ''in vitro'') '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response).  
  
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]
+
[[File:GT138-Fig1-V3.jpg|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]
  
  

Revision as of 19:21, 5 February 2025

Under construction icon-blue-48px.png

This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Glycosyltransferase Family GT138
Clan Fido fold
Mechanism Inverting
Active site residues Known
CAZy DB link
https://www.cazy.org/GT138.html


Substrate specificities

GT138 family of glycosyltransferase is exemplified by AvrB [1] that contains a Fido domain [2] (Fig. 1A). AvrB is different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation [3], phosphorylation [4], UMPylation [5], and phosphocholination [6, 7]. Therefore, AvrB is a unique Fido protein that functions as a glycosyltransferase. As a bacterial effector from the plant pathogen Pseudomonas syringae, AvrB utilizes host UDP-rhamnose (or dTDP-rhamnose in vitro) as a co-substrate to modify the host protein RIN4 and causes the programmed cell death (namely hypersensitive response).

File:GT138-Fig1-V3.jpg
Figure 1. Glycosyltransferase folds. (A) Fido fold (left) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. (B) Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.


Kinetics and Mechanism

Content is to be added here.

Catalytic Residues

Content is to be added here.

Three-dimensional structures

Content is to be added here.

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

Error fetching PMID 38354245:
Error fetching PMID 19503829:
Error fetching PMID 19039103:
Error fetching PMID 24141193:
Error fetching PMID 22504181:
Error fetching PMID 21822290:
Error fetching PMID 23572077:
  1. Error fetching PMID 38354245: [Peng2024]
  2. Error fetching PMID 19503829: [Kinch2009]
  3. Error fetching PMID 19039103: [Yarbrough2009]
  4. Error fetching PMID 24141193: [Castro-Roa2013]
  5. Error fetching PMID 22504181: [Feng2012]
  6. Error fetching PMID 21822290: [Mukherjee2011]
  7. Error fetching PMID 23572077: [Campanacci2013]

All Medline abstracts: PubMed