A0A7Z3C0X0 · A0A7Z3C0X0_PSEFL

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 site66Fe3+ (UniProtKB | ChEBI)
Binding site66Zn2+ (UniProtKB | ChEBI)
Binding site68Fe3+ (UniProtKB | ChEBI)
Binding site68Zn2+ (UniProtKB | ChEBI)
Binding site754-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site1384-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site138N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site1714-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site236Fe3+ (UniProtKB | ChEBI)
Binding site236Zn2+ (UniProtKB | ChEBI)
Binding site2394-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site311Fe3+ (UniProtKB | ChEBI)
Binding site311Zn2+ (UniProtKB | ChEBI)
Binding site313N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site315N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site3164-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
      C6Y56_01830

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • G7
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A7Z3C0X0

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain57-374Amidohydrolase-related

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    401
  • Mass (Da)
    43,279
  • Last updated
    2021-06-02 v1
  • Checksum
    BF9D9EB11BFE0AC0
MKTLWQHCHVATMAQGVYSIIEDAAIVTSGALIEWIGPRSQLPSGEYPAVNDLQGAWVTPGLIDCHTHTVFGGNRSGEFEKRLQGVSYAEIAAAGGGIASTVRATREASEDELFASAAKRLKSLMRDGVTTVEMKSGYGLDLASERKILRVIRRLAAELPISVRSTCLAAHALPPEYKDRADDYIDHICAEMLPALAAEGLVDAVDAFCEYLAFSPEQVERVFIAAQKLGLPVKLHAEQLSSLHGSSLAARYHALSADHLEFMDEADAIAMAESDTVAVLLPGAFYFLRETQLPPMEALRKHKVKIAIASDLNPGTSPALSLRLMLNMACTCFRMTPEEALAGATIHAAQALGMAETHGSLEAGKVADFVAWQIDRPADLAYWLGGELDKRVVRHGVESSL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP027561
EMBL· GenBank· DDBJ
QJP93379.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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