A0A7Y2Z1P1 · A0A7Y2Z1P1_9GAMM

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site71Fe3+ (UniProtKB | ChEBI)
Binding site71Zn2+ (UniProtKB | ChEBI)
Binding site73Fe3+ (UniProtKB | ChEBI)
Binding site73Zn2+ (UniProtKB | ChEBI)
Binding site804-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site1434-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site143N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site1764-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site241Fe3+ (UniProtKB | ChEBI)
Binding site241Zn2+ (UniProtKB | ChEBI)
Binding site2444-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site315Fe3+ (UniProtKB | ChEBI)
Binding site315Zn2+ (UniProtKB | ChEBI)
Binding site317N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site319N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site3204-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
    • ORF names
      HKO99_14885

Organism names

Accessions

  • Primary accession
    A0A7Y2Z1P1

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain62-403Amidohydrolase-related

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    403
  • Mass (Da)
    43,359
  • Last updated
    2021-06-02 v1
  • Checksum
    31BDD83E6F1D4624
MPVLHNIAQLATCPRGNPQNDAGLIANAAIAWEEDIIRWVGHAPDLPPEFRNEPSIDCEQRLVIPGLIDCHTHLCFGGWRGDEFALRIAGATYQEIAEAGGGINSTVTATRAASLGQLRRKAATILDRMLELGITTVECKSGYGLDLANELKQLEVYRQLNQAHVVDLIPTFLGAHVVPKEHTGSRDRYIELLCNELIPMIARENLALFCDAFIEDGAFTGSEARRILSCAASHGLGIKIHADQLSTGGGAELAAELRAVSAEHLEYISDEGIEALAQSGTVAVSLPLASCYLDEAYIPARKLISAGVPVAVATDFNPGSAPSFHLPLAMTLACIHQRMTPEEVLNGVTTVAARAVCADDRIGSLLPGFRADLALIDAPSLNHWLYHFVPNACLKVLKNGKWI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABDPX010000082
EMBL· GenBank· DDBJ
NNK52879.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
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