Q3AE33 · THIC_CARHZ
- ProteinPhosphomethylpyrimidine synthase
- GenethiC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids429 (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 | 66 | substrate | ||||
Sequence: N | ||||||
Binding site | 95 | substrate | ||||
Sequence: M | ||||||
Binding site | 124 | substrate | ||||
Sequence: Y | ||||||
Binding site | 163 | substrate | ||||
Sequence: H | ||||||
Binding site | 185-187 | substrate | ||||
Sequence: SRG | ||||||
Binding site | 226-229 | substrate | ||||
Sequence: DGLR | ||||||
Binding site | 265 | substrate | ||||
Sequence: E | ||||||
Binding site | 269 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 292 | substrate | ||||
Sequence: Y | ||||||
Binding site | 333 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 409 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 412 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 416 | [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
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Thermoanaerobacterales > Thermoanaerobacteraceae > Carboxydothermus
Accessions
- Primary accessionQ3AE33
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000242250 | 1-429 | Phosphomethylpyrimidine synthase | |||
Sequence: MTQLLKAKEGVITREMEVVAAEERKSPEEIRQKVALGEVVIPANVNHQNLHPKGIGAGLKVKVNANLGTSENRCFYEDELKKVKVAIKAGADAIMDLSTGGNLDEIRRAIIKESSVPVGTVPLYQAAAETLNKYGDISRLDPELLFDVIEKQAADGVDFMTVHVGVTREILKVLDRFPRVTEVVSRGGSLTIAWMEKNGRENPLYEQFDRLLAICRKYDVTLSLGDGLRPGSIADATDQLQIMELMKLGELVKYAQNQGVQVMVEGPGHVPINQIEMNVKLMKRLCANAPFYVLGPLVTDIAPGYDHITAAIGGAWAAYFGADFLCYVTPAEHLGLPTVEDVEEGVIALKIAAHAADLARGNREAWNRDYEMSVARKELNWERQFELAINPERARKMRIERGSQDIKSCSMCGELCAMKIMNERGGKNA |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length429
- Mass (Da)47,317
- Last updated2005-11-22 v1
- ChecksumBBC7386CF65BF7D7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000141 EMBL· GenBank· DDBJ | ABB14730.1 EMBL· GenBank· DDBJ | Genomic DNA |