A0A2U8DLJ3 · A0A2U8DLJ3_9CLOT
- ProteinThiamine-phosphate synthase
- GenethiE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids204 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
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; 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: QVREK | ||||||
Binding site | 69 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 70 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 89 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 108 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 134-136 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: TGT | ||||||
Binding site | 137 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 165 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 185-186 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: IS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | magnesium ion binding | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionA0A2U8DLJ3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-188 | Thiamine phosphate synthase/TenI | ||||
Sequence: LYLITDRSFLKGRSLKNVVEEAILGGVTLIQVREKNISTREFYNVALEVKEVTKYYKVPIIINDRIDIAQAIDADGVHLGQSDMHIKIARKILGEEKIIGISAGNVKEAVDAERDGADYLGIGAVFYTGTKKDIETPIGIKGLKEVCNSVKIPSVAIGGINETNFKEVLSTGTNGISVISAI |
Sequence similarities
Belongs to the thiamine-phosphate synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length204
- Mass (Da)22,250
- Last updated2018-09-12 v1
- ChecksumAF2440F10EF84A23
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP020953 EMBL· GenBank· DDBJ | AWI03301.1 EMBL· GenBank· DDBJ | Genomic DNA |