|Gene:||thiF||Accession Number: BSU11700 (MetaCyc)|
Synonyms: yjbU, adenylate transferase and sulfur transferase
Species: Bacillus subtilis subtilis 168
The ThiF protein is involved in the posttranslational modification of ThiS by the conversion of the carboxylic acid group of the carboxyl-terminal glycine into a thiocarboxylate [Taylor98]. More specifically, ThiF catalyzes the adenylation of the carboxyl-terminal glycine of ThiS by ATP [Begley99, Taylor98]. ThiS and ThiF form a covalently linked protein-protein conjugate as an essential intermediate of this reaction [Xi01].
The thiF gene of Bacillus subtilis has been cloned, expressed in Escherichia coli and purified, and used in an in vitro reconstitution reaction for production of the thiazole moiety of thiamin phosphate [Park03a]. When ThiS was incubated with ThiF and ATP, the formation of a carboxy-adenylated-[ThiS sulfur-carrier protein] was observed by ESI-FTMS. Unlike in Escherichia coli, no cross-linking between ThiF and ThiS has been detected [Park03a].
|Map Position: [1,245,808 -> 1,246,818]|
Molecular Weight of Polypeptide: 36.4 kD (from nucleotide sequence)
Unification Links: DBTBS Operons:thiF , Entrez:2633524 , GenoList (SubtiList):BSU11700 , GOA:O31619 , HSSP:1JW9 , Mint:MINT-8367236 , Protein Model Portal:O31619 , SMR:O31619 , String:224308.BSU11700 , String:BSU11700 , SubtilisWiki:thiF , SubtiWiki:thiF , UniProt:O31619
|Biological Process:||GO:0008152 - metabolic process
GO:0009228 - thiamine biosynthetic process [GOA00]
|Molecular Function:||GO:0000166 - nucleotide binding
GO:0003824 - catalytic activity [GOA01a]
GO:0005488 - binding [GOA01a]
GO:0005524 - ATP binding [GOA00]
GO:0016740 - transferase activity [GOA00]
GO:0016779 - nucleotidyltransferase activity [GOA00, GOA01]
GO:0046872 - metal ion binding [GOA00]
Enzymatic reaction of: [sulfur-carrier protein ThiS] adenylyltransferase
EC Number: 126.96.36.199
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
Begley99: Begley TP, Downs DM, Ealick SE, McLafferty FW, Van Loon AP, Taylor S, Campobasso N, Chiu HJ, Kinsland C, Reddick JJ, Xi J (1999). "Thiamin biosynthesis in prokaryotes." Arch Microbiol 1999;171(5);293-300. PMID: 10382260
Park03a: Park JH, Dorrestein PC, Zhai H, Kinsland C, McLafferty FW, Begley TP (2003). "Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1)." Biochemistry 42(42);12430-8. PMID: 14567704
Taylor98: Taylor SV, Kelleher NL, Kinsland C, Chiu HJ, Costello CA, Backstrom AD, McLafferty FW, Begley TP (1998). "Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation." J Biol Chem 273(26);16555-60. PMID: 9632726
Xi01: Xi J, Ge Y, Kinsland C, McLafferty FW, Begley TP (2001). "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 U S A 98(15);8513-8. PMID: 11438688
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493