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 See a page that's out-of-date and just needs a touch-up?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.

Glycosyltransferase Family 138

From CAZypedia
Jump to navigation Jump to search
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]. 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) [1, 2].

AvrB contains a Fido domain [3, 4] (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 [5, 6, 7, 8] (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation [9], phosphorylation [10], UMPylation [11], and phosphocholination [12, 13]. Therefore, AvrB is a unique Fido protein that functions as a glycosyltransferase.

Figure 1. Glycosyltransferase folds. (A) Fido fold (left [4]) 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

AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A). AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent.

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
The first structure of GT138 family (Fido type) is the crystal structure of AvrB [3].

References

  1. Peng W, Garcia N, Servage KA, Kohler JJ, Ready JM, Tomchick DR, Fernandez J, and Orth K. (2024). Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4. Sci Adv. 2024;10(7):eadd5108. DOI:10.1126/sciadv.add5108 | PubMed ID:38354245 [Peng2024]
  2. Mackey D, Holt BF 3rd, Wiig A, and Dangl JL. (2002). RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis. Cell. 2002;108(6):743-54. DOI:10.1016/s0092-8674(02)00661-x | PubMed ID:11955429 [Mackey2002]
  3. Lee CC, Wood MD, Ng K, Andersen CB, Liu Y, Luginbühl P, Spraggon G, and Katagiri F. (2004). Crystal structure of the type III effector AvrB from Pseudomonas syringae. Structure. 2004;12(3):487-94. DOI:10.1016/j.str.2004.02.013 | PubMed ID:15016364 [Lee2004]
  4. Kinch LN, Yarbrough ML, Orth K, and Grishin NV. (2009). Fido, a novel AMPylation domain common to fic, doc, and AvrB. PLoS One. 2009;4(6):e5818. DOI:10.1371/journal.pone.0005818 | PubMed ID:19503829 [Kinch2009]
  5. Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL, and Seeberger PH. (2022). 2022. DOI:10.1101/9781621824213 | PubMed ID:35536922 [Varki2022]
  6. Lairson LL, Henrissat B, Davies GJ, and Withers SG. (2008). Glycosyltransferases: structures, functions, and mechanisms. Annu Rev Biochem. 2008;77:521-55. DOI:10.1146/annurev.biochem.76.061005.092322 | PubMed ID:18518825 [Lairson2008]
  7. Zhang H, Zhu F, Yang T, Ding L, Zhou M, Li J, Haslam SM, Dell A, Erlandsen H, and Wu H. (2014). The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold. Nat Commun. 2014;5:4339. DOI:10.1038/ncomms5339 | PubMed ID:25023666 [Zhang2014]
  8. Sernee MF, Ralton JE, Nero TL, Sobala LF, Kloehn J, Vieira-Lara MA, Cobbold SA, Stanton L, Pires DEV, Hanssen E, Males A, Ward T, Bastidas LM, van der Peet PL, Parker MW, Ascher DB, Williams SJ, Davies GJ, and McConville MJ. (2019). A Family of Dual-Activity Glycosyltransferase-Phosphorylases Mediates Mannogen Turnover and Virulence in Leishmania Parasites. Cell Host Microbe. 2019;26(3):385-399.e9. DOI:10.1016/j.chom.2019.08.009 | PubMed ID:31513773 [Sernee2019]
  9. Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, and Orth K. (2009). AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science. 2009;323(5911):269-72. DOI:10.1126/science.1166382 | PubMed ID:19039103 [Yarbrough2009]
  10. Castro-Roa D, Garcia-Pino A, De Gieter S, van Nuland NAJ, Loris R, and Zenkin N. (2013). The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu. Nat Chem Biol. 2013;9(12):811-7. DOI:10.1038/nchembio.1364 | PubMed ID:24141193 [Castro-Roa2013]
  11. Feng F, Yang F, Rong W, Wu X, Zhang J, Chen S, He C, and Zhou JM. (2012). A Xanthomonas uridine 5'-monophosphate transferase inhibits plant immune kinases. Nature. 2012;485(7396):114-8. DOI:10.1038/nature10962 | PubMed ID:22504181 [Feng2012]
  12. Mukherjee S, Liu X, Arasaki K, McDonough J, Galán JE, and Roy CR. (2011). Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature. 2011;477(7362):103-6. DOI:10.1038/nature10335 | PubMed ID:21822290 [Mukherjee2011]
  13. Campanacci V, Mukherjee S, Roy CR, and Cherfils J. (2013). Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain. EMBO J. 2013;32(10):1469-77. DOI:10.1038/emboj.2013.82 | PubMed ID:23572077 [Campanacci2013]

All Medline abstracts: PubMed