A0A1W1USU0 · A0A1W1USU0_9PAST
- ProteinPhosphomethylpyrimidine synthase
- GenethiC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids639 (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 | 244 | substrate | |||
Binding site | 273 | substrate | |||
Binding site | 302 | substrate | |||
Binding site | 338 | substrate | |||
Binding site | 358-360 | substrate | |||
Binding site | 399-402 | substrate | |||
Binding site | 438 | substrate | |||
Binding site | 442 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 465 | substrate | |||
Binding site | 506 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 586 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 589 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 594 | [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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Pasteurella
Accessions
- Primary accessionA0A1W1USU0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Structure
Sequence
- Sequence statusComplete
- Length639
- Mass (Da)71,490
- Last updated2017-06-07 v1
- Checksum66D1AA024F03E3A4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FWWV01000013 EMBL· GenBank· DDBJ | SMB83794.1 EMBL· GenBank· DDBJ | Genomic DNA |