A0A2J0SY25 · A0A2J0SY25_STEMA
- ProteinPhosphomethylpyrimidine synthase
- GenethiC
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids614 (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 | 230 | substrate | ||||
Sequence: N | ||||||
Binding site | 259 | substrate | ||||
Sequence: M | ||||||
Binding site | 288 | substrate | ||||
Sequence: Y | ||||||
Binding site | 324 | substrate | ||||
Sequence: H | ||||||
Binding site | 344-346 | substrate | ||||
Sequence: SRG | ||||||
Binding site | 385-388 | substrate | ||||
Sequence: DGLR | ||||||
Binding site | 424 | substrate | ||||
Sequence: E | ||||||
Binding site | 428 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 451 | substrate | ||||
Sequence: Y | ||||||
Binding site | 492 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 572 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 575 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 580 | [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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Lysobacteraceae > Stenotrophomonas > Stenotrophomonas maltophilia group
Accessions
- Primary accessionA0A2J0SY25
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MNAQLSALQQQAQQLSESVTR | ||||||
Region | 1-36 | Disordered | ||||
Sequence: MNAQLSALQQQAQQLSESVTRPIPGSRKIHVPGSRP | ||||||
Domain | 22-99 | ThiC-associated | ||||
Sequence: PIPGSRKIHVPGSRPDLQVPMREIALTRTPTLFGGEENAPVTVYDTSGPYTDPQARVDLSAGLPALRRAWIEERGDTE |
Sequence similarities
Belongs to the ThiC family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length614
- Mass (Da)68,237
- Last updated2018-03-28 v1
- ChecksumA1B60D14640857FE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MNAQLSALQQQAQQLSESVTR |