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Glycosyltransferase Family 138
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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.
![](/images/thumb/9/90/GT138-Fig1-V3.png/1300px-GT138-Fig1-V3.png)
Kinetics and Mechanism
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Catalytic Residues
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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
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- First catalytic nucleophile identification
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- First general acid/base residue identification
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- First 3-D structure
- The first structure of GT138 family (Fido type) is the crystal structure of AvrB [3].
References
- 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 |
- 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 |
- 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 |
- 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 |
- 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 |
- 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 |
- 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 |
- 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 |
- 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 |
- 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 |
- 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 |
- 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 |
- 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 |