A0A9D1PUJ7 · A0A9D1PUJ7_9BACT

Function

function

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

Caution

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

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 site6Nucleophile
Binding site244[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site291Mg2+ (UniProtKB | ChEBI)
Binding site353Mg2+ (UniProtKB | ChEBI)
Binding site354Mg2+ (UniProtKB | ChEBI)
Binding site390[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site440[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site443[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      purF
    • ORF names
      H9894_01280

Organism names

Accessions

  • Primary accession
    A0A9D1PUJ7

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-226Glutamine amidotransferase type-2

Sequence similarities

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

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    463
  • Mass (Da)
    52,437
  • Last updated
    2023-05-03 v1
  • Checksum
    6C4DAA096F27E381
MIHHSCGLFAVYGHEDASRLTYFGLYAQQHRGQESCGIVSRAEDGHCYQYKGMGLVPDVFEEKHLQKLKGTVALGHVRYSTTGRPSIINAQPLMIHYKDKYIAIAHNGNLVNAVDLRRELEDDGAVFMATSDTEVIMHVFVRELAKHDVIDAVRATCNKLRGAYCLLFLIDDTLVAVRDPYGFHPLSLGRLDKAPVLASETCAFDLMEAEYEHNIRPGEMYVISPDGEMSLNLTDNMPERPRQCIFELVYFARPDSYIFGEQVYQCRKQMGWQLAHESTPDADFIMPFPDSGVYPAIGFAQSAEIPYEHAMIRNHYVGRTFIQPSQSMRNFGVRVKINPVREMIDGKRICIVDDSIVRGTTMSTRVKKLRELGAKEVHIRISCPPVRFPCYYGIDFASPKELIAANYSLDEIKKILDVDSLHFLSKEGLLRSVMHEDQYCTACFDGDYPVKPCSLYGKFGLES

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DXHV01000015
EMBL· GenBank· DDBJ
HIV99813.1
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.
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