A0A7Z3C0X0 · A0A7Z3C0X0_PSEFL
- ProteinImidazolonepropionase
- GenehutI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids401 (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 | 66 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 66 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 68 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 68 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 75 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 138 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 138 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 171 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 236 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 236 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 239 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 311 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 311 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 313 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 315 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 316 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A7Z3C0X0
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 57-374 | Amidohydrolase-related | ||||
Sequence: WVTPGLIDCHTHTVFGGNRSGEFEKRLQGVSYAEIAAAGGGIASTVRATREASEDELFASAAKRLKSLMRDGVTTVEMKSGYGLDLASERKILRVIRRLAAELPISVRSTCLAAHALPPEYKDRADDYIDHICAEMLPALAAEGLVDAVDAFCEYLAFSPEQVERVFIAAQKLGLPVKLHAEQLSSLHGSSLAARYHALSADHLEFMDEADAIAMAESDTVAVLLPGAFYFLRETQLPPMEALRKHKVKIAIASDLNPGTSPALSLRLMLNMACTCFRMTPEEALAGATIHAAQALGMAETHGSLEAGKVADFVAWQI |
Sequence similarities
Belongs to the metallo-dependent hydrolases superfamily. HutI family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length401
- Mass (Da)43,279
- Last updated2021-06-02 v1
- ChecksumBF9D9EB11BFE0AC0