EC number:2.7.7.73

Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.7 Nucleotidyltransferases
ID:2.7.7.73
Description:Sulfur carrier protein ThiS adenylyltransferase.
Cath: 3.40.50.720;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.7.73
BRENDA Enzyme Link: BRENDA 2.7.7.73
KEGG Enzyme Link: KEGG2.7.7.73
BioCyc Enzyme Link: BioCyc 2.7.7.73
ExPASy Enzyme Link: ExPASy2.7.7.73
EC2PDB Enzyme Link: EC2PDB 2.7.7.73
ExplorEnz Enzyme Link: ExplorEnz 2.7.7.73
PRIAM enzyme-specific profiles Link: PRIAM 2.7.7.73
IntEnz Enzyme Link: IntEnz 2.7.7.73
MEDLINE Enzyme Link: MEDLINE 2.7.7.73

EC number:2.7.7.73

MSA:

2.7.7.73;
Phylogenetic Tree:

2.7.7.73;
Uniprot:
M-CSA:
RHEA:43344 [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + ATP + H(+) = [sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + diphosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8].[H+;H0:9]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis.Lehmann C, Begley TP, Ealick SE2006 Jan 1016388576
Structural analysis of Escherichia coli ThiF.Duda DM, Walden H, Sfondouris J, Schulman BA2005 Jun 1715896804
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.Xi J, Ge Y, Kinsland C, McLafferty FW, Begley TP2001 Jul 1711438688