A0A328L779 · A0A328L779_9BACI

  • Protein
    Phosphoribosyl-AMP cyclohydrolase
  • Gene
    hisI
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

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

Note: Binds 1 Mg2+ ion per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site71Mg2+ (UniProtKB | ChEBI)
Binding site72Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site73Mg2+ (UniProtKB | ChEBI)
Binding site75Mg2+ (UniProtKB | ChEBI)
Binding site88Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site95Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionmagnesium ion binding
Molecular Functionphosphoribosyl-AMP cyclohydrolase activity
Molecular Functionzinc ion binding
Biological ProcessL-histidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoribosyl-AMP cyclohydrolase
  • EC number
  • Short names
    PRA-CH

Gene names

    • Name
      hisI
    • ORF names
      B5P42_29260

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SRB_331
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus

Accessions

  • Primary accession
    A0A328L779

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain24-97Phosphoribosyl-AMP cyclohydrolase

Sequence similarities

Belongs to the PRA-CH family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    101
  • Mass (Da)
    11,539
  • Last updated
    2018-10-10 v1
  • Checksum
    482BE0517E68866C
MKPNFAKGLIPAVVIEEDTKEVLMLAYMNEEAYDKTLETKRTWFYSRSRQSLWNKGGTSGNVQYVQSLYLDCDQDAIVVVVKQVGPACHTGEKTCFHYKII

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NADV01000064
EMBL· GenBank· DDBJ
RAN72406.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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