D7WCS3 · D7WCS3_9CORY

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.

Caution

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

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
    • ORF names
      HMPREF0291_11611

Organism names

Accessions

  • Primary accession
    D7WCS3

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain49-187ATP phosphoribosyltransferase catalytic
Domain208-278Histidine biosynthesis HisG C-terminal

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    283
  • Mass (Da)
    30,163
  • Last updated
    2010-10-05 v1
  • Checksum
    FE368A0FF3B321F9
MIKIAVPNKGSLSEAATGILKEAGYKGRGYTKALNIVDEANGVEFFFLRPKDIAIYVAGGHLDLGITGRDLMLDSRADVEEILDLGFGGSTFRFAAPADVAESMTIADLEGKRLATSYPHLAADYLADRGINAEVIRLDGAVEIAIKLGVADAIADVVSTGATLHQQGLAPFGEPIVASEAIVVKRTGRELTVEDEIVLSRIRGILTAHNFVMLDYNVSRDNLQSAVDITPGLTGPTVSPLQRENWVAVRAMVPRKEANLLMDRLAAAGAEAILASELKIARI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACLJ02000003
EMBL· GenBank· DDBJ
EFK53954.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp