A0A162GII9 · A0A162GII9_LACPN
- ProteinPhosphoribosyl-AMP cyclohydrolase
- GenehisI
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids108 (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 | 73 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 74 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 75 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 77 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 90 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 97 | 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
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactiplantibacillus
Accessions
- Primary accessionA0A162GII9
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-99 | Phosphoribosyl-AMP cyclohydrolase | ||||
Sequence: MVAWMNAESYQRTLASGQTWLWSRSRQELWHKGATSGNLQDVVSMTLDCDQDTLLVAVHPHGPACHTGHTSCFF |
Sequence similarities
Belongs to the PRA-CH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length108
- Mass (Da)11,902
- Last updated2016-07-06 v1
- ChecksumC0DA9975E0B29F2C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LUXM01000026 EMBL· GenBank· DDBJ | KZU95450.1 EMBL· GenBank· DDBJ | Genomic DNA |