A0KF84 · HUTI_AERHH
- ProteinImidazolonepropionase
- GenehutI
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids411 (go to sequence)
- Protein existenceEvidence at protein level
- 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 | 75 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 75 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 77 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 77 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 84 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 147 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 147 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 180 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 245 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 245 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 248 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 320 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 320 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 322 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 324 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 325 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: T |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Aeromonadales > Aeromonadaceae > Aeromonas
Accessions
- Primary accessionA0KF84
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000306422 | 1-411 | Imidazolonepropionase | |||
Sequence: MNKELLNCERVWLNVTPATLRSDLADYGLLEPHALGVHEGRIHALVPMQDLKGPYPAHWQDMKGKLVTPGLIDCHTHLIFAGSRAEEFELRQKGVPYAEIARKGGGIISTVRATRAACEEQLFELALPRVKSLIREGVTTVEIKSGYGLTLEDELKMLRVARRLGEALPIRVKTTLLAAHAVPPEYRDDPDSWVETICQEIIPAAAEAGLADAVDVFCEHIGFSLAQTEQVYLAADQYGLAVKGHMDQLSNLGGSTLAANFGALSVDHLEYLDPEGIQALAHRGVVATLLPTAFYFLKETKLPPVAALRKAGVPMAVSSDINPGTAPIVSLRMAMNMACTLFGLTPVEAMAGVTRHAARALGEQEQLGQLRVGMLADFLVWNCGHPAELSYLIGVDQLVSRVINGEETLHG |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length411
- Mass (Da)44,543
- Last updated2007-10-02 v2
- Checksum63D38DB562DC8EBF
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000462 EMBL· GenBank· DDBJ | ABK39901.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |