C0E0G1 · C0E0G1_9CORY
- ProteinThiamine-phosphate synthase
- GenethiD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids730 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic activity
- 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H+ = CO2 + diphosphate + thiamine phosphate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 37-41 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: QLRDK | ||||||
Binding site | 78 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 79 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 97 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 116 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 149-151 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: TET | ||||||
Binding site | 152 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 183 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 201-202 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: VS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | hydroxymethylpyrimidine kinase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphomethylpyrimidine kinase activity | |
Molecular Function | thiamine-phosphate diphosphorylase activity | |
Biological Process | thiamine biosynthetic process | |
Biological Process | thiamine diphosphate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThiamine-phosphate synthase
- EC number
- Short namesTP synthase ; TPS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium
Accessions
- Primary accessionC0E0G1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-204 | Thiamine phosphate synthase/TenI | ||||
Sequence: LYLVTDPGSDPDAVPAIVTQAITGGVTVVQLRDKHATKPQIRQRAQALKDAIQAVTAVSNADPSTIPLFINDHVDIAAELGLHAHIGQGDLSYVAARRQLPAELMLGLSIETADQLEHVVETCHASGVRLPDVVGIGPVRATETKPDHATPLGVARVQRIARMAAAHGIKSVAIGGVDKHIAAELQQVDGVCVVSAI | ||||||
Domain | 238-487 | Pyridoxamine kinase/Phosphomethylpyrimidine kinase | ||||
Sequence: DPTGGAGAQADLKSIAAAGGYGMNAITALVAQNTHGVRSIHTPPLSFLREQLDAVVSDVTIDAVKIGMLGSADIVACVRQWLAEHPMPLVVLDPVMVATSGDRLLDPDAEQAVIEFAHHVDIVTPNVPELAVLLSAPEPARTFEEALSQAAEFAQKSNTIVIAKGGHLDGKLANNAVVYPDGRITTITTPRIDTTNTHGTGCSLSSALATRLAAGDTITEAIEWVSYWLADSIRAGAALEVGTPGGHGPI | ||||||
Domain | 528-726 | Thiaminase-2/PQQC | ||||
Sequence: WDSMGEVWSQIMGLPFIMGLRDGSLSKREFDFYLNQDAHYLANYSRALAVLAAKAGEPQYQVEWAESARDCLVVEAQLHHEWLGGISGDTSPVTLGYTNFLTATAYGDDYVVGAAAVLPCYWIYAEVGACLAASNHPDHPYHEWLKTYGDQSFVTTTEAALRRVEHALVQATGVQRAAATAAFQVACAYEREFFDQASR |
Sequence similarities
Belongs to the thiamine-phosphate synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length730
- Mass (Da)77,752
- Last updated2009-05-05 v1
- Checksum030EF0BA7A4670B5