A0A927JE65 · A0A927JE65_9ACTN
- ProteinPhosphomethylpyrimidine synthase
- GenethiC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids556 (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 | 154 | substrate | ||||
Sequence: N | ||||||
Binding site | 183 | substrate | ||||
Sequence: M | ||||||
Binding site | 212 | substrate | ||||
Sequence: Y | ||||||
Binding site | 248 | substrate | ||||
Sequence: H | ||||||
Binding site | 268-270 | substrate | ||||
Sequence: SRG | ||||||
Binding site | 309-312 | substrate | ||||
Sequence: DGLR | ||||||
Binding site | 348 | substrate | ||||
Sequence: E | ||||||
Binding site | 352 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 375 | substrate | ||||
Sequence: Y | ||||||
Binding site | 416 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 496 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 499 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 504 | [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 > Actinomycetota > Actinomycetes > Mycobacteriales > Hoyosellaceae > Lolliginicoccus
Accessions
- Primary accessionA0A927JE65
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length556
- Mass (Da)61,241
- Last updated2023-02-22 v1
- Checksum6CCCF13B57F7B914
Keywords
- Technical term