thiC

thiC
168

4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase, biosynthesis of the pyrimidine moiety of thiamine

Locus
BSU_08790
Molecular weight
65.74 kDa
Isoelectric point
5.26
Protein length
590 aaSequenceBlast
Gene length
1773 bpSequenceBlast
Function
biosynthesis of thiamine
Product
4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase
Essential
no
Synonyms
thiC, thiA
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0422 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
955,895  957,667
The protein
Catalyzed reaction/ biological activity
5-amino-1-(5-phospho-β-D-ribosyl)imidazole + S-adenosyl-L-methionine --> 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H+ + L-methionine (according to UniProt)
Protein family
thiC family (single member, according to UniProt)
Cofactors
Fe-S cluster PubMed
Structure
3EPN (PDB) (from Caulobacter crescentus, 65% identity) PubMed
P45740 (AlphaFold)
Modification
phosphorylated on Arg-556 PubMed
phosphorylated on Ser-565, Ser-586 and Tyr-589 PubMed
Additional information
subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and Regulation
Operons
Genes
thiC
Description
PubMed
Regulation
repressed by thiamine (Thi-box) PubMed
the Thi-box RNA is degraded by RNase Y PubMed
Regulatory mechanism
Thi-box: RNA switch, in Thi-box regulon
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thiC

2025-04-07 11:24:29

Jstuelk

59

912da64c2149c634effa834239fc89e9aaa6bc4a

848AEFB0DD859F65873E9FA627981725B72E955A

Biological materials
Mutant
1A603 ( thiC::erm), PubMed, available at BGSC
BKE08790 (thiC::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATTACTTTTCCTTCCCCTT,  downstream forward: _UP4_TAAAAAAAATGAAGATGGAG
BKK08790 (thiC::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATTACTTTTCCTTCCCCTT,  downstream forward: _UP4_TAAAAAAAATGAAGATGGAG
Two-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
References
Reviews
Jurgenson CT, Begley TP, Ealick SE The structural and biochemical foundations of thiamin biosynthesis. Annual review of biochemistry. 2009; 78:569-603. doi:10.1146/annurev.biochem.78.072407.102340. PMID:19348578
Begley TP, Downs DM, Ealick SE, McLafferty FW, Van Loon AP, Taylor S, Campobasso N, Chiu HJ, Kinsland C, Reddick JJ, Xi J Thiamin biosynthesis in prokaryotes. Archives of microbiology. 1999 Apr; 171(5):293-300. . PMID:10382260
Original Publications
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Page visits: 7247

Time of last update: 2025-04-09 18:09:59

Author of last update: Melvin.boenninger