Q9RQ83 · HIS1_BUCMH

Function

function

Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Feedback inhibited by histidine.

Pathway

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

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP phosphoribosyltransferase activity
Molecular Functionmagnesium ion binding
Biological ProcessL-histidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP phosphoribosyltransferase
  • EC number
  • Short names
    ATP-PRT
    ; ATP-PRTase

Gene names

    • Name
      hisG

Organism names

Accessions

  • Primary accession
    Q9RQ83

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001518371-299ATP phosphoribosyltransferase

Interaction

Subunit

Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme.

Structure

Family & Domains

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    299
  • Mass (Da)
    33,710
  • Last updated
    2000-05-01 v1
  • Checksum
    576213A51CEA6D50
MIHNNRLRIVMQKNWKLSSDSKDLLVRCGIKINLCKQKLIAFSENMPIDVMCVRDDDIPGLIMDGIVDIGIIGENVLEEEVLSRKLRLDSVDYIKLKRLDFGVCRLSLAVPIDKEYTDIYCLNNSRIATSYPHLLKKYFDKKNIIFKSCMLNGSVEVAPRAGLSDAICDLVSTGATLEANGLREVQIIFRSKACLICKTGNISVEKQNVINTLMTRIQGVIKARESKYIMLHAPIKKLEEVIDLLHGAERPTILKLAGDDSRVAMHMVSSETLFWETMEKLKLLGASSILVLPIEKMME

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF129283
EMBL· GenBank· DDBJ
AAF13775.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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