B8JBF9 · HUTI_ANAD2
- ProteinImidazolonepropionase
- GenehutI
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids421 (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 | 76 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 76 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 78 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 78 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 85 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 148 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 148 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 182 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 247 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 247 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 250 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 324 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 326 | N-formimidoyl-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 327 | 4-imidazolone-5-propanoate (UniProtKB | ChEBI) | ||||
Sequence: S |
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 > Myxococcota > Myxococcia > Myxococcales > Cystobacterineae > Anaeromyxobacteraceae > Anaeromyxobacter
Accessions
- Primary accessionB8JBF9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000133876 | 1-421 | Imidazolonepropionase | |||
Sequence: MSRPTATLVLRNAVVATCDRSPSDAGLLPGAAVAVEGRRVAWVGRDRDLEAEVNAGGAQVIDARGGLVTPGLVDSHTHLVFAGERAGEFALRCAGRSYLQVALSGGGIAVTTRATRAAPDEQLLADAAARARRLIAQGVTTIEVKSGYGLDAPEELRLLRIVHQLGDALGGDATILPTLLFHAVPPEQVGDRAAFVREACAALIPQVARERLAVFCDVFVEDGAFAPDEARRLLQAAKDRGLVPRVHAEQLTAGGGARLAAELGCASADHLEELDDAGVAALAEARVVAGLLPLSTLFLGSERYAPARRLLEAGVPVSLATNMNPGSAMSENVGLTLSLACLKLGLTPAEALVAFTAGGARALRQPDLGRIARGADADLVLWGCGSPEHLAWHMAVNHALVVVKHGRVVHEAPSAAMVDCR |
Structure
Sequence
- Sequence statusComplete
- Length421
- Mass (Da)43,731
- Last updated2009-03-03 v1
- Checksum21E3FFEFC04A19C6
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001359 EMBL· GenBank· DDBJ | ACL65786.1 EMBL· GenBank· DDBJ | Genomic DNA |