A0A2D3D3I1 · A0A2D3D3I1_9BIFI
- ProteinThiamine-phosphate synthase
- GenethiE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids514 (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+ = thiamine phosphate + CO2 + diphosphate
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 | 48-52 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | |||
Binding site | 84 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | |||
Binding site | 85 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 109 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 128 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | |||
Binding site | 157-159 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 160 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | |||
Binding site | 193 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 213-214 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | |||
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 | phosphorylation | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium
Accessions
- Primary accessionA0A2D3D3I1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 18-216 | Thiamine phosphate synthase/TenI | |||
Domain | 264-508 | Pyridoxamine kinase/Phosphomethylpyrimidine kinase | |||
Sequence similarities
Belongs to the thiamine-phosphate synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length514
- Mass (Da)53,432
- Last updated2018-01-31 v1
- MD5 ChecksumFD6154BFF40441E4255C4406D397A5A6
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP018044 EMBL· GenBank· DDBJ | ATU19638.1 EMBL· GenBank· DDBJ | Genomic DNA |