B8JBF9 · HUTI_ANAD2

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

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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.

TypeIDPosition(s)Description
Binding site76Fe3+ (UniProtKB | ChEBI)
Binding site76Zn2+ (UniProtKB | ChEBI)
Binding site78Fe3+ (UniProtKB | ChEBI)
Binding site78Zn2+ (UniProtKB | ChEBI)
Binding site854-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site1484-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site148N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site1824-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site247Fe3+ (UniProtKB | ChEBI)
Binding site247Zn2+ (UniProtKB | ChEBI)
Binding site2504-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site324N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site326N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site3274-imidazolone-5-propanoate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionimidazolonepropionase activity
Molecular Functioniron ion binding
Molecular Functionzinc ion binding
Biological ProcessL-histidine catabolic process to glutamate and formamide
Biological ProcessL-histidine catabolic process to glutamate and formate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Imidazolonepropionase
  • EC number
  • Alternative names
    • Imidazolone-5-propionate hydrolase

Gene names

    • Name
      hutI
    • Ordered locus names
      A2cp1_2448

Organism names

Accessions

  • Primary accession
    B8JBF9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001338761-421Imidazolonepropionase

Structure

Family & Domains

Sequence similarities

Belongs to the metallo-dependent hydrolases superfamily. HutI family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    421
  • Mass (Da)
    43,731
  • Last updated
    2009-03-03 v1
  • Checksum
    21E3FFEFC04A19C6
MSRPTATLVLRNAVVATCDRSPSDAGLLPGAAVAVEGRRVAWVGRDRDLEAEVNAGGAQVIDARGGLVTPGLVDSHTHLVFAGERAGEFALRCAGRSYLQVALSGGGIAVTTRATRAAPDEQLLADAAARARRLIAQGVTTIEVKSGYGLDAPEELRLLRIVHQLGDALGGDATILPTLLFHAVPPEQVGDRAAFVREACAALIPQVARERLAVFCDVFVEDGAFAPDEARRLLQAAKDRGLVPRVHAEQLTAGGGARLAAELGCASADHLEELDDAGVAALAEARVVAGLLPLSTLFLGSERYAPARRLLEAGVPVSLATNMNPGSAMSENVGLTLSLACLKLGLTPAEALVAFTAGGARALRQPDLGRIARGADADLVLWGCGSPEHLAWHMAVNHALVVVKHGRVVHEAPSAAMVDCR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001359
EMBL· GenBank· DDBJ
ACL65786.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp