A0A8J7YXW0 · A0A8J7YXW0_9CYAN

  • Protein
    Amidophosphoribosyltransferase
  • Gene
    purF
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site34Nucleophile
Binding site278[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site325Mg2+ (UniProtKB | ChEBI)
Binding site387Mg2+ (UniProtKB | ChEBI)
Binding site388Mg2+ (UniProtKB | ChEBI)
Binding site424[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site475[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site478[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
      GS601_02335

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • A
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Leptolyngbyales > Leptolyngbyaceae > Myxacorys > Myxacorys almedinensis

Accessions

  • Primary accession
    A0A8J7YXW0

Proteomes

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-22Polar residues
Region1-29Disordered
Domain34-262Glutamine 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
    506
  • Mass (Da)
    54,665
  • Last updated
    2022-05-25 v1
  • Checksum
    92EC910D4BD75FA0
MLPNDPPSDQSACASTPTPETPALSPSDKPEEACGVFGVYSPGETVATLAYFGLYALQHRGQESAGIAAFDGNQVNLHKDMGLVSQVFNETILSKLPGALAVGHTRYSTTGSSRVVNAQPAIVPTRLGSLALAHNGNLVNTAQLRAELSQRDHTFITTTDSEMIALALGDEVNDGKSWVDAAASAFQRCSGAFSLVIGTPDGLLGTRDRNGIRPLVLGTLPKDDPELPNRYVLASETCGLDIIGADYVRDIQPGELVWITAEGLTSIQWAKKAERKLCIFEMIYFARPDSVMHDESLYSYRLRIGRQLAQESYVDADIVIAVPDSGIPAAIGFSQESGIPYAEGLIKNRYVGRTFIQPTQGMREAGIRMKLNPLKDVLAGKRVVIVDDSIVRGTTSRKIVKALRDAGAIEVHMRISSPPVTHPCFYGIDTDSQDHLIAATKSVADIAQQIGVDSLQYLSWEGMLTATRENTNSFCSACFTGEYPISVPEQLKRAKLILEKEKVAPV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-22Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WVIE01000002
EMBL· GenBank· DDBJ
NDJ16134.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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