Q2RST7 · THIC_RHORT
- ProteinPhosphomethylpyrimidine synthase
- GenethiC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids621 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Catalytic activity
- 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + CO + 5'-deoxyadenosine + formate + L-methionine + 3 H+
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 215 | substrate | |||
Binding site | 244 | substrate | |||
Binding site | 273 | substrate | |||
Binding site | 309 | substrate | |||
Binding site | 329-331 | substrate | |||
Binding site | 370-373 | substrate | |||
Binding site | 409 | substrate | |||
Binding site | 413 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 436 | substrate | |||
Binding site | 477 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 557 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 560 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 565 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | carbon-carbon lyase activity | |
Molecular Function | zinc ion binding | |
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 namePhosphomethylpyrimidine synthase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae > Rhodospirillum
Accessions
- Primary accessionQ2RST7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000242298 | 1-621 | Phosphomethylpyrimidine synthase | ||
Interaction
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | |||
Region | 1-29 | Disordered | |||
Sequence similarities
Belongs to the ThiC family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length621
- Mass (Da)66,602
- Last updated2006-01-24 v1
- Checksum73ED29E7D7D1C7F9
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000230 EMBL· GenBank· DDBJ | ABC22808.1 EMBL· GenBank· DDBJ | Genomic DNA |