ExplorEnz: EC 2.7.7.73

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2.7.7.73

Accepted name:

sulfur carrier protein ThiS adenylyltransferase

Reaction:

ATP + [ThiS] = diphosphate + adenylyl-[ThiS]

Other name(s):

thiF (gene name)

Systematic name:

ATP:[ThiS] adenylyltransferase

Comments:

Binds Zn²⁺. The enzyme catalyses the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine. The enzyme shows significant structural similarity to ubiquitin-activating enzyme [3,4]. In Escherichia coli, but not in Bacillus subtilis, the enzyme forms a cross link from Cys-184 to the ThiS carboxy terminus (the position that is also thiolated) via an acyldisulfide [2].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Taylor, S.V., Kelleher, N.L., Kinsland, C., Chiu, H.J., Costello, C.A., Backstrom, A.D., McLafferty, F.W. and Begley, T.P. Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation. J. Biol. Chem. 273 (1998) 16555–16560. [DOI] [PMID: 9632726]
2.	Xi, J., Ge, Y., Kinsland, C., McLafferty, F.W. and Begley, T.P. Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein^--protein conjugate that is functionally analogous to the ubiquitin/E1 complex. Proc. Natl. Acad. Sci. USA 98 (2001) 8513–8518. [DOI] [PMID: 11438688]
3.	Duda, D.M., Walden, H., Sfondouris, J. and Schulman, B.A. Structural analysis of Escherichia coli ThiF. J. Mol. Biol. 349 (2005) 774–786. [DOI] [PMID: 15896804]
4.	Lehmann, C., Begley, T.P. and Ealick, S.E. Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis. Biochemistry 45 (2006) 11–19. [DOI] [PMID: 16388576]

[EC 2.7.7.73 created 2011]