A0A0F5EII1 · A0A0F5EII1_ACIBA

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 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
      F4T83_08700
      , FJU42_19765
      , LV35_01939

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • AB2828
    • MRSN14237
    • AMA24
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter > Acinetobacter calcoaceticus/baumannii complex

Accessions

  • Primary accession
    A0A0F5EII1

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain57-397Amidohydrolase-related

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    401
  • Mass (Da)
    44,059
  • Last updated
    2015-06-24 v1
  • MD5 Checksum
    9391E58316A997703092AACB970E1CE1
MKKLWQNCHIATMQNGQYSYIEDAAIVTEGHLIHWIGKQQQLPADTYSETVDLNGAWVTPGFIDCHTHSVFGGNRSVEFEKRLQGVSYAEIAASGGGIASTVRATREASEEQLLNSALKRIRCMQQDGVTTIEIKSGYGLNYENERKMLRVIRQIGEKLPMTVKSTCLAAHALPPEYKDQSDAYIEHICTEMLPKLHAEGLVDAVDAFCEHLAFSPAQVERVFKTAQSLNLPVKLHAEQLSSLGGSSLAARYHALSADHLEYMTEDDVKAMAASGTIAVLLPGAFYLLRETQYPPIESLIKHGVRIALSSDLNPGTSPALSLRLMLNMGSTLFRLTPEQALAGVTIHAAQALGLEQTHGSLEQGKVADFVAWDIEHPSEIVYWLGGDLPKRVVQHGQEVIF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LRDT01000025
EMBL· GenBank· DDBJ
KZA17471.1
EMBL· GenBank· DDBJ
Genomic DNA
VYTJ01000010
EMBL· GenBank· DDBJ
MRA06799.1
EMBL· GenBank· DDBJ
Genomic DNA
VHGY01000084
EMBL· GenBank· DDBJ
TPU60068.1
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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