A0A7L4QG02 · A0A7L4QG02_9EURY

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
      GKC00_01885
      , GKC01_02155

Organism names

Accessions

  • Primary accession
    A0A7L4QG02

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain49-209ATP phosphoribosyltransferase catalytic
Domain214-286Histidine biosynthesis HisG C-terminal

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    289
  • Mass (Da)
    31,910
  • Last updated
    2021-04-07 v1
  • Checksum
    21E1B1CB5485DECC
MMLKIGLPKGSLQESTLNMFKKAGYSINISSRSYKPSIDDTNIECLLIRAQEIPRYVEKGIIDIGLTGLDWVIENNADVVNVGKLVYAKQGLKPVRWVLAVSDSSKIKTIEDLNGKRIATEVVNITKKYLTDKGVDASVEFSWGATEVKVPELVDAIVDLTETGSSLKANNLRVLDTLLESTTVLISNKESWKSSWKRKKTEDLFMLLKGALAAESMVGVKMNVQKSNLEEVISVLPALRKPTISNLSSDGWVAVETIVDEKIIRDLIPKLKSAGAEGIIEYPLNKVIY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAEEM010000059
EMBL· GenBank· DDBJ
NYT03439.1
EMBL· GenBank· DDBJ
Genomic DNA
JAAEEN010000032
EMBL· GenBank· DDBJ
NYT13295.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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