A0A377UZM0 · A0A377UZM0_KLEPN

  • Protein
    Imidazolonepropionase
  • Gene
    hutI
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site106Fe3+ (UniProtKB | ChEBI)
Binding site106Zn2+ (UniProtKB | ChEBI)
Binding site108Fe3+ (UniProtKB | ChEBI)
Binding site108Zn2+ (UniProtKB | ChEBI)
Binding site1154-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site1784-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site178N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site2114-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site276Fe3+ (UniProtKB | ChEBI)
Binding site276Zn2+ (UniProtKB | ChEBI)
Binding site2794-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site351Fe3+ (UniProtKB | ChEBI)
Binding site351Zn2+ (UniProtKB | ChEBI)
Binding site353N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site355N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site3564-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
      NCTC13443_02648

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NCTC13443
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella

Accessions

  • Primary accession
    A0A377UZM0

Proteomes

Subcellular Location

Keywords

Family & Domains

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    439
  • Mass (Da)
    47,967
  • Last updated
    2018-11-07 v1
  • Checksum
    89B22E7A966868F1
MVFSHKKITFPCAIVDFTGVMKINVYTTHDKLSAMTEATSELVIWRNGRLATLNPDHAQPYGLLERHALLVRDGRIAAIVAEDDVPSGRSIDLEGRLVTPGLIDCHTHLVFGGSRAQEWEQRLNGVSYQTISASGGGINSTVRATRDSSEAELLAVAQPRLERLLREGVTTLEIKSGYGLDLPNERKMLRVARQLADHNGVELSATLLSAHATPPEYQGDANGYITLVCETILPTLWQEGLFESVDVFCENVGFSPQQTERVFQAAQALGIPVKGHVEQLSSLGGAQLVSRYHGLSADHIEYLTEEGVAAMRESGTVAALLPGAFYFLNETRKPPVELLRKYQVPMAVATDFNPGTSPFASLHLAMNMACVKFGLTPEEAWAGVTRHAARALGRQASHGQLAPGFVANFAIWDAEHPVEMVYEPGRSPLWHRVVQGELQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UGKT01000001
EMBL· GenBank· DDBJ
STT02298.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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