Accession | TIGR04271 |
Name | ThiI_C_thiazole |
Function | thiazole biosynthesis domain |
Gene Symbol | thiI |
Trusted Cutoff | 70.00 |
Domain Trusted Cutoff | 70.00 |
Noise Cutoff | 55.00 |
Domain Noise Cutoff | 40.00 |
Isology Type | equivalog_domain |
HMM Length | 101 |
Author | Haft DH |
Entry Date | Jan 25 2012 11:58AM |
Last Modified | Feb 10 2012 10:37AM |
Comment | The ThiI protein of Escherichia coli is a bifunctional protein in which most of the length of the protein is responsible for sulfurtransferase activity in 4-thiouridine modification to tRNA (EC 2.8.1.4 - see model TIGR00342). This rhodanese-like C-terminal domain, by itself, is able to synthesize the thiazole moiety during thiamin biosynthesis. Note that the invariant Cys residue in this domain is unusual in being required for both activities of the bifunctional ThiI protein. |
References | RN [1]
RM PMID:21724998
RT The rhodanese domain of ThiI is both necessary and sufficient for synthesis of the thiazole moiety of thiamine in Salmonella enterica.
RA Martinez-Gomez NC, Palmer LD, Vivas E, Roach PL, Downs DM
RL J Bacteriol. 2011 Sep;193(18):4582-7. Epub 2011 Jul 1. |
Genome Property | GenProp0250: thiamine: hydroxyethylthiazole from 1-deoxy-D-xylulose-5-phosphate, cysteine, either Tyr or Gly (HMM) |