A0A0D6H327 · A0A0D6H327_STAAU

  • 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 site76Fe3+ (UniProtKB | ChEBI)
Binding site76Zn2+ (UniProtKB | ChEBI)
Binding site78Fe3+ (UniProtKB | ChEBI)
Binding site78Zn2+ (UniProtKB | ChEBI)
Binding site854-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site1484-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site148N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site1814-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site242Fe3+ (UniProtKB | ChEBI)
Binding site242Zn2+ (UniProtKB | ChEBI)
Binding site2454-imidazolone-5-propanoate (UniProtKB | ChEBI)
Binding site317Fe3+ (UniProtKB | ChEBI)
Binding site317Zn2+ (UniProtKB | ChEBI)
Binding site319N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site321N-formimidoyl-L-glutamate (UniProtKB | ChEBI)
Binding site3224-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
    • Synonyms
      hutI_1
    • ORF names
      ACR74_08735
      , C0102_04805
      , CNH36_13045
      , EIG96_01665
      , EP54_11490
      , EQ90_01725
      , GO814_07825
      , GO942_01565
      , HMPREF3211_02171
      , LB359_13200
      , NCTC10702_03653
      , NCTC13131_01674
      , SAMEA1029512_01063
      , SAMEA1029528_01928
      , SAMEA1029536_00862
      , SAMEA2078260_00149
      , SAMEA2078588_00456
      , SAMEA2080344_00471
      , SAMEA2081063_01464
      , SAMEA4008575_00951
      , SAMEA4552975_02096
      , SAMEA70146418_00403

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • CA15
    • M121
    • MRSA_S20
    • PSS7673
    • Newman
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    A0A0D6H327
  • Secondary accessions
    • A0A1E8XCK4

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain67-402Amidohydrolase-related

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    412
  • Mass (Da)
    45,039
  • Last updated
    2015-05-27 v1
  • Checksum
    9CBBB04A4EC54600
MNDLIINHIAELILPRSTDKPLKGKELDELNVVKNGTVVIKDGKIVYAGTHTDDYDATETIDASGKVVSPALVDAHTHLTFGGSREHEMSLKRQGKSYLEILEMGGGILSTVNATRETSEDDLFKKAEHDLLTMIKHGVLAVESKSGYGLDRENELKQLKVSNRLAEKYDLDMKHTFLGPHAVPKEASSNEAFLEEMIALLPEVKQYADFADIFCETGVFTIEQSQHYMQKAKEAGFKVKIHADEIDPLGGLELAIDEQAISADHLVASSDKGKEKLRNSDTVAVLLPATTFYLGKEDYADARGMLDNNGAIALATDYNPGSSVTNNLQLVMAIAALKLKLSPNEVWNAVTVNAAKAIDINAGTINTGDKANLVIWDAPNHEYIPYHFGINHAEKVIKDGKVIVDNTVSFKA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP023391
EMBL· GenBank· DDBJ
ATC72504.1
EMBL· GenBank· DDBJ
Genomic DNA
CACTOE010000006
EMBL· GenBank· DDBJ
CAA4107372.1
EMBL· GenBank· DDBJ
Genomic DNA
CACTPG010000005
EMBL· GenBank· DDBJ
CAA4121676.1
EMBL· GenBank· DDBJ
Genomic DNA
CACTPI010000008
EMBL· GenBank· DDBJ
CAA4138561.1
EMBL· GenBank· DDBJ
Genomic DNA
CACTQT010000001
EMBL· GenBank· DDBJ
CAA4266818.1
EMBL· GenBank· DDBJ
Genomic DNA
CACTWD010000008
EMBL· GenBank· DDBJ
CAA4684028.1
EMBL· GenBank· DDBJ
Genomic DNA
CACUNS010000002
EMBL· GenBank· DDBJ
CAA6048708.1
EMBL· GenBank· DDBJ
Genomic DNA
CACURZ010000002
EMBL· GenBank· DDBJ
CAA6314044.1
EMBL· GenBank· DDBJ
Genomic DNA
CAIGXB010000002
EMBL· GenBank· DDBJ
CAC5784029.1
EMBL· GenBank· DDBJ
Genomic DNA
CAIHOM010000003
EMBL· GenBank· DDBJ
CAC7013392.1
EMBL· GenBank· DDBJ
Genomic DNA
CAIIGD010000001
EMBL· GenBank· DDBJ
CAC8194810.1
EMBL· GenBank· DDBJ
Genomic DNA
UAUZ02000002
EMBL· GenBank· DDBJ
CAD7354141.1
EMBL· GenBank· DDBJ
Genomic DNA
LALJ01000003
EMBL· GenBank· DDBJ
KMR38199.1
EMBL· GenBank· DDBJ
Genomic DNA
LALQ01000052
EMBL· GenBank· DDBJ
KMR56331.1
EMBL· GenBank· DDBJ
Genomic DNA
LFVK01000004
EMBL· GenBank· DDBJ
KSA77330.1
EMBL· GenBank· DDBJ
Genomic DNA
LRQH01000160
EMBL· GenBank· DDBJ
KXA33632.1
EMBL· GenBank· DDBJ
Genomic DNA
JAIUEN010000139
EMBL· GenBank· DDBJ
MCE3363270.1
EMBL· GenBank· DDBJ
Genomic DNA
WPTS01000027
EMBL· GenBank· DDBJ
MVK35044.1
EMBL· GenBank· DDBJ
Genomic DNA
WPXC01000004
EMBL· GenBank· DDBJ
MVM09379.1
EMBL· GenBank· DDBJ
Genomic DNA
PKSU01000003
EMBL· GenBank· DDBJ
PZL80765.1
EMBL· GenBank· DDBJ
Genomic DNA
RQSX01000030
EMBL· GenBank· DDBJ
RZH96441.1
EMBL· GenBank· DDBJ
Genomic DNA
UHBY01000003
EMBL· GenBank· DDBJ
SUL37638.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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