A0A328L779 · A0A328L779_9BACI
- ProteinPhosphoribosyl-AMP cyclohydrolase
- GenehisI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids101 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic activity
- 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 1 zinc ion per subunit.
Pathway
Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 71 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 72 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 73 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 75 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 88 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 95 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoribosyl-AMP cyclohydrolase activity | |
Molecular Function | zinc ion binding | |
Biological Process | L-histidine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoribosyl-AMP cyclohydrolase
- EC number
- Short namesPRA-CH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0A328L779
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-97 | Phosphoribosyl-AMP cyclohydrolase | ||||
Sequence: MLAYMNEEAYDKTLETKRTWFYSRSRQSLWNKGGTSGNVQYVQSLYLDCDQDAIVVVVKQVGPACHTGEKTCFH |
Sequence similarities
Belongs to the PRA-CH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length101
- Mass (Da)11,539
- Last updated2018-10-10 v1
- Checksum482BE0517E68866C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NADV01000064 EMBL· GenBank· DDBJ | RAN72406.1 EMBL· GenBank· DDBJ | Genomic DNA |