A0A4U0QJE9 · A0A4U0QJE9_9RHOB

  • 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 site76Mg2+ (UniProtKB | ChEBI)
Binding site77Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site78Mg2+ (UniProtKB | ChEBI)
Binding site80Mg2+ (UniProtKB | ChEBI)
Binding site93Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site100Zn2+ (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
      FA740_16165

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CCTCC AB2016182
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Paracoccus

Accessions

  • Primary accession
    A0A4U0QJE9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain29-102Phosphoribosyl-AMP cyclohydrolase

Sequence similarities

Belongs to the PRA-CH family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    118
  • Mass (Da)
    13,001
  • Last updated
    2019-07-31 v1
  • Checksum
    4F83B229C468B15F
MFDPLSLKYDAAGLIPAIAQDAASGEVLMMAWMNADAVARTLSTGRVTYWSRSRASFWIKGESSGHVQQLVEMRVDCDRDCLLVLVEQTGPACHTNRRSCFYTGIRDGAEVVLSEPMV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SUNH01000027
EMBL· GenBank· DDBJ
TJZ81835.1
EMBL· GenBank· DDBJ
Genomic DNA

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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