P28173 · PUR1_CHICK

  • Protein
    Amidophosphoribosyltransferase
  • Gene
    PPAT
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster per subunit.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; N1-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site12Nucleophile
Binding site280[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site327Mg2+ (UniProtKB | ChEBI)
Binding site389Mg2+ (UniProtKB | ChEBI)
Binding site390Mg2+ (UniProtKB | ChEBI)
Binding site426[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site496[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site499[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionamidophosphoribosyltransferase activity
Molecular Functionmetal ion binding
Biological Process'de novo' IMP biosynthetic process
Biological Processglutamine metabolic process
Biological Processpurine nucleobase biosynthetic process
Biological Processpurine nucleotide biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Amidophosphoribosyltransferase
  • EC number
  • Short names
    ATase
  • Alternative names
    • Glutamine phosphoribosylpyrophosphate amidotransferase
      (GPAT
      )

Gene names

    • Name
      PPAT
    • Synonyms
      GPAT

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus

Accessions

  • Primary accession
    P28173

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for propeptide, chain.

TypeIDPosition(s)Description
PropeptidePRO_00000292811-11
ChainPRO_000002928212-510Amidophosphoribosyltransferase

Proteomic databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-261Glutamine amidotransferase type-2

Sequence similarities

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    510
  • Mass (Da)
    56,257
  • Last updated
    1992-12-01 v1
  • Checksum
    F4371FE1FEC7C744
MELEELGIREECGVFGCIAAGVWPTELDVPHVITLGLVGLQHRGQESAGIVTSDGESSQAFKVHKGMGLINHVFNADSLKKLYVSNLGIGHTRYSTSGISELQNCQPFVVETLHGKIAVAHNGELTNAVRLRRKLMRHGVGLSTSSDSELITQLLAFTPPLENDDTADWVARIKNLMNETPTSYSLLIMHKDIIYAVRDPYGNRPLCIGRLIPVGDINGKGKDNSETEGWVVSSESCSFLSIGAEYYREVLPGEIVKISRYDVQTLDVVPRPEGDPSAFCIFEYVYFARPDSIFEGQMVYSVRRRCGQQLAIEAPVEADLVSTVPESATPAALGYAQKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRVVIIDDSIVRGNTISPIIKLLRESGAKEVHIRVASPPIRFPCYMGINIPTKEELIANRPEFHDLANYIGADSVVYLSVEGLVSSVQESIKARKENENSLKTQKSRVGKIGHCTACLTGDYPVELEW

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M60069
EMBL· GenBank· DDBJ
AAA62736.1
EMBL· GenBank· DDBJ
mRNA
L12533
EMBL· GenBank· DDBJ
AAA17895.1
EMBL· GenBank· DDBJ
Unassigned DNA

Genome annotation databases

Similar Proteins

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