A0A2I8VEQ3 · A0A2I8VEQ3_9EURY
- ProteinImidazolonepropionase
- GenehutI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids419 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic activity
- 4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate
Cofactor
Fe3+ (UniProtKB | Rhea| CHEBI:29034 )
Note: Binds 1 zinc or iron ion per subunit.
Pathway
Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 82 | Fe3+ (UniProtKB | ChEBI) | |||
Binding site | 82 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 84 | Fe3+ (UniProtKB | ChEBI) | |||
Binding site | 84 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 91 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | |||
Binding site | 154 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | |||
Binding site | 154 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 187 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | |||
Binding site | 250 | Fe3+ (UniProtKB | ChEBI) | |||
Binding site | 250 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 253 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | |||
Binding site | 324 | Fe3+ (UniProtKB | ChEBI) | |||
Binding site | 324 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 326 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | imidazolonepropionase activity | |
Molecular Function | iron ion binding | |
Molecular Function | zinc ion binding | |
Biological Process | L-histidine catabolic process to glutamate and formamide | |
Biological Process | L-histidine catabolic process to glutamate and formate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameImidazolonepropionase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Salinigranum
Accessions
- Primary accessionA0A2I8VEQ3
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 37-59 | Aminodeoxyfutalosine deaminase/Imidazolonepropionase-like composite | |||
Domain | 73-416 | Amidohydrolase-related | |||
Sequence similarities
Belongs to the metallo-dependent hydrolases superfamily. HutI family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length419
- Mass (Da)44,106
- Last updated2018-03-28 v1
- MD5 Checksum82675A27C5D036D868551C508A71885D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP026309 EMBL· GenBank· DDBJ | AUV80407.1 EMBL· GenBank· DDBJ | Genomic DNA |