Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A4S1GWV8 · A0A4S1GWV8_UNCXX

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 site84Fe3+ (UniProtKB | ChEBI)
Binding site84Zn2+ (UniProtKB | ChEBI)
Binding site86Fe3+ (UniProtKB | ChEBI)
Binding site86Zn2+ (UniProtKB | ChEBI)
Binding site934-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site1564-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site156N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site1894-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site254Fe3+ (UniProtKB | ChEBI)
Binding site254Zn2+ (UniProtKB | ChEBI)
Binding site2574-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site329Fe3+ (UniProtKB | ChEBI)
Binding site329Zn2+ (UniProtKB | ChEBI)
Binding site331N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site333N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site3344-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
      EN811_24555

Organism names

Accessions

  • Primary accession
    A0A4S1GWV8

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain75-394Amidohydrolase-related

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    419
  • Mass (Da)
    44,279
  • Last updated
    2019-07-31 v1
  • MD5 Checksum
    065AF459387E74CEF908285F16C4F473
MPGNKSAKGAAMGNATALWRNARLATFDPLREGIGAVEKGVIAVSSGRIAFAGPESDLPAYLAAAEEITDCDGRWITPALIDCHTHLVFGGNRAMEFEMRLNGATYEEIAKAGGGIVSSVRSTRAVSEDVLMAQALPRLDTLLSEGVSTIEIKSGYGLDIDTELKMLRVARRLETLRPVRIVTSYLAAHATPAEYKGRNGDYITDVVLPGLEKAQAEGLVDAVDGFCEGIAFSVEEIARVFEKARQLGLPVKLHAEQLSNLGGAALAASCGGLSADHLEYLDESGARALAKAGTVAVLLPGAFYALREKQAPPMQALRDAGATIALATDCNPGTSPLTSLLLTMNMGATLFRMTVEECLAATTRNAAKALGLLAETGTLEAGKSADLAIWDIERPAELVYRIGFNPLHARIFKGQKVSP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SRTJ01000010
EMBL· GenBank· DDBJ
TGV44091.1
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.
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.
Help