P00499 · HIS1_SALTY

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 (By similarity).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Feedback inhibited by histidine. Also inhibited by AMP and ADP.

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
    • Ordered locus names
      STM2071

Organism names

Accessions

  • Primary accession
    P00499

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001518641-299ATP phosphoribosyltransferase

Proteomic databases

Expression

Induction

Repressed by ppGpp in the presence of histidine.

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 (Probable).

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    299
  • Mass (Da)
    33,212
  • Last updated
    1986-07-21 v1
  • Checksum
    EE165D90C49B36F8
MLDNTRLRIAIQKSGRLSDDSRELLARCGIKINLHTQRLIAMAENMPIDILRVRDDDIPGLVMDGVVDLGIIGENVLEEELLNRRAQGEDPRYLTLRRLDFGGCRLSLATPVDEAWDGPAALDGKRIATSYPHLLKRYLDQKGVSFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEANGLREVEVIYRSKACLIQRDGEMAQSKQELIDKLLTRIQGVIQARESKYIMMHAPSERLEEVIALLPGAERPTILPLAGEQQRVAMHMVSSETLFWETMEKLKALGASSILVLPIEKMME

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X13464
EMBL· GenBank· DDBJ
CAA31822.1
EMBL· GenBank· DDBJ
Genomic DNA
J01804
EMBL· GenBank· DDBJ
AAA88614.1
EMBL· GenBank· DDBJ
Genomic DNA
M28367
EMBL· GenBank· DDBJ
AAA27142.1
EMBL· GenBank· DDBJ
Genomic DNA
AE006468
EMBL· GenBank· DDBJ
AAL20975.1
EMBL· GenBank· DDBJ
Genomic DNA
V01371
EMBL· GenBank· DDBJ
CAA24657.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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