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A0A2I8VEQ3 · A0A2I8VEQ3_9EURY

  • 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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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 site82Fe3+ (UniProtKB | ChEBI)
Binding site82Zn2+ (UniProtKB | ChEBI)
Binding site84Fe3+ (UniProtKB | ChEBI)
Binding site84Zn2+ (UniProtKB | ChEBI)
Binding site914-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site1544-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site154N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site1874-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site250Fe3+ (UniProtKB | ChEBI)
Binding site250Zn2+ (UniProtKB | ChEBI)
Binding site2534-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site324Fe3+ (UniProtKB | ChEBI)
Binding site324Zn2+ (UniProtKB | ChEBI)
Binding site326N-formimidoyl-L-glutamate (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
      C2R22_01005

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • GX10
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Salinigranum

Accessions

  • Primary accession
    A0A2I8VEQ3

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain37-59Aminodeoxyfutalosine deaminase/Imidazolonepropionase-like composite
Domain73-416Amidohydrolase-related

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    419
  • Mass (Da)
    44,106
  • Last updated
    2018-03-28 v1
  • MD5 Checksum
    82675A27C5D036D868551C508A71885D
MTPTLDLVVHDAREVVVGPDENENGDDDGLRRHENAGIAVVDGRVAAVGPTNELRRAYPPENARESLDATGKTVVPGFVDAHTHACFAGDRSDEFEAKLRGASYGELLAQGGGILRTVRAVRETSTRELTADLLAHLDVMLAHGTTTVEVKSGYGLDTETELRMLRAMADADDAHPVDVVPTFMGAHAVPQGRTGDDYVEDVVCEQLPAVADQGIARFCDVFCDEGAFTPEQSRRVLDAGRDHGLTPKVHAEELAHTGGARLASQVEAASADHLLRATAADVEALVDADVVPVLLPGTAFSLGGDYADARAMLDAGAPAALATDFNPNCFARSMPFAMTLACVGMRLTPAEALVAATAHAARALDFGAGPGGGERGTLREDAPADLAVVDAPSHTHLAYDFDVNRVERVVKGGEVVHRD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP026309
EMBL· GenBank· DDBJ
AUV80407.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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