A0A2V3EIF8 · A0A2V3EIF8_ECOLX

  • Protein
    Histidine biosynthesis bifunctional protein HisB
  • Gene
    hisB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site9Nucleophile
Binding site9Mg2+ (UniProtKB | ChEBI)
Active site11Proton donor
Binding site11Mg2+ (UniProtKB | ChEBI)
Binding site93Zn2+ (UniProtKB | ChEBI)
Binding site95Zn2+ (UniProtKB | ChEBI)
Binding site101Zn2+ (UniProtKB | ChEBI)
Binding site103Zn2+ (UniProtKB | ChEBI)
Binding site130Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionhistidinol-phosphatase activity
Molecular Functionimidazoleglycerol-phosphate dehydratase activity
Molecular Functionmetal ion binding
Biological ProcessL-histidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histidine biosynthesis bifunctional protein HisB

Including 2 domains:

  • Recommended name
    Histidinol-phosphatase
  • EC number
  • Recommended name
    Imidazoleglycerol-phosphate dehydratase
  • EC number
  • Short names
    IGPD

Gene names

    • Name
      hisB
    • ORF names
      BANRA_02797
      , CCS08_00755

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • ECA-B
    • Ecoli022
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A2V3EIF8

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-166Histidinol-phosphatase
Region167-355Imidazoleglycerol-phosphate dehydratase

Sequence similarities

In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.
In the N-terminal section; belongs to the histidinol-phosphatase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    355
  • Mass (Da)
    40,277
  • Last updated
    2018-09-12 v1
  • Checksum
    0A4ECC2941D91DD1
MSQKYLFIDRDGTLISEPPSDFQVDRFDKLAFEPGVIPELLKLQKAGYKLVMITNQDGLGTQSFPQADFDGPHNLMMQIFTSQGVQFDEVLICPHLPADECDCRKPKVKLVERYLAEQAMDRANSYVIGDRATDIQLAENMGINGLRYDRETLNWPMIGEQLTKRDRYAHVVRNTKETQIDVQVWLDREGGSKINTGVGFFDHMLDQIATHGGFRMEINVKGDLYIDDHHTVEDTALALGEALKIALGDKRGICRFGFVLPMDECLARCALDISGRPHLEYKAEFTYQRVGDLSTEMIEHFFRSLSYTMGVTLHLKTKGKNDHHRVESLFKAFGRTLRQAIRVEGDTLPSSKGVL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NHTF01000004
EMBL· GenBank· DDBJ
OWW57218.1
EMBL· GenBank· DDBJ
Genomic DNA
UWXJ01000001
EMBL· GenBank· DDBJ
VCY84123.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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