Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Characterization of thiI, a new gene involved in thiazole biosynthesis in Salmonella typhimurium.
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Salmonella typhimurium thiI is required for synthesis of the thiazole (THZ) moiety of thiamine; genetic characterisation only.
"We present herein the initial characterization of thiI, a gene required for THZ synthesis."
The rhodanese domain of ThiI is both necessary and sufficient for synthesis of the thiazole moiety of thiamine in Salmonella enterica.
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The rhodanese domain of Salmonella ThiI is sufficient for thiazole synthesis; s4U-specific residues are not needed. Short ThiI lacking the rhodanese domain is unlikely to work in thiazole synthesis.
"the C-terminal rhodanese domain of ThiI was sufficient for thiazole synthesis in vivo"
Functional Analysis of Bacillus subtilis Genes Involved in the Biosynthesis of 4-Thiouridine in tRNA.
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B. subtilis ThiI (no rhodanese domain) is needed for s4U but not thiamine.
"Gene inactivation experiments in B. subtilis indicate the requirement of ThiI and NifZ for the biosynthesis of 4-thiouridine, but not thiamine."
Biosynthesis of 4-thiouridine in tRNA in the methanogenic archaeon Methanococcus maripaludis.
Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA.
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E. coli ThiI receives IscS persulfide sulfur, binds tRNA and makes s4U.
"ThiI is a recipient of S(0) from IscS and catalyzes the ultimate sulfur transfer step in the biosynthesis of s(4)U"
Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate.
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E. coli ThiI Cys456 in the rhodanese domain is essential for s4U.
"Mutation of Cys-456 to alanine impairs this sulfurtransferase activity, and the C456A ThiI is incapable of supporting generation of 4-thiouridine in tRNA both in vitro and in vivo."
The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA.
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E. coli ThiI Cys344 is essential and forms a disulfide with Cys456 during turnover.
"Substitution of Cys-344, the only cysteine residue conserved among all sequenced ThiI, resulted in the loss of function in vivo and a 2700-fold reduction in activity measured in vitro."
TudS desulfidases recycle 4-thiouridine-5'-monophosphate at a catalytic [4Fe-4S] cluster.
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In P. putida KT2440, thiI deletion drastically reduces tRNA s4U.
"As expected, the content of 4-thiouridine in bulk tRNA was drastically reduced in the ΔthiI knockout strain (negative control)."