A0A267TF83 · A0A267TF83_9BACT
- ProteinPhosphomethylpyrimidine synthase
- GenethiC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids619 (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 + 5'-deoxyadenosine + CO + formate + 3 H+ + L-methionine
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 | 226 | substrate | ||||
Sequence: N | ||||||
Binding site | 255 | substrate | ||||
Sequence: M | ||||||
Binding site | 284 | substrate | ||||
Sequence: Y | ||||||
Binding site | 320 | substrate | ||||
Sequence: H | ||||||
Binding site | 340-342 | substrate | ||||
Sequence: SRG | ||||||
Binding site | 381-384 | substrate | ||||
Sequence: DGLR | ||||||
Binding site | 420 | substrate | ||||
Sequence: E | ||||||
Binding site | 424 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 447 | substrate | ||||
Sequence: Y | ||||||
Binding site | 488 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 568 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 571 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 576 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C |
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 > Bacteroidota > Cytophagia > Cytophagales > Flectobacillaceae > Flectobacillus
Accessions
- Primary accessionA0A267TF83
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-96 | ThiC-associated | ||||
Sequence: PFPNSRKIYVPGALHNIQVAMREISLTDTKISGNIFTKNPSVAVYDTSGPYTDPNIEIDVRKGLPKLREEWIIARGDTE |
Sequence similarities
Belongs to the ThiC family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length619
- Mass (Da)68,734
- Last updated2017-12-20 v1
- Checksum6D98B8AF980B44C2
Keywords
- Technical term