A6QFS7 · PURL_STAAE

Function

function

Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.

Catalytic activity

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide: step 1/2.

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site54
Binding site57ATP (UniProtKB | ChEBI)
Binding site96ATP (UniProtKB | ChEBI)
Binding site98Mg2+ 1 (UniProtKB | ChEBI)
Binding site99-102substrate
Active site100Proton acceptor
Binding site121substrate
Binding site122Mg2+ 2 (UniProtKB | ChEBI)
Binding site245substrate
Binding site273Mg2+ 2 (UniProtKB | ChEBI)
Binding site317-319substrate
Binding site495ATP (UniProtKB | ChEBI)
Binding site532ATP (UniProtKB | ChEBI)
Binding site533Mg2+ 1 (UniProtKB | ChEBI)
Binding site535substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionphosphoribosylformylglycinamidine synthase activity
Biological Process'de novo' IMP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoribosylformylglycinamidine synthase subunit PurL
  • EC number
  • Short names
    FGAM synthase
  • Alternative names
    • Formylglycinamide ribonucleotide amidotransferase subunit II
      (FGAR amidotransferase II
      ; FGAR-AT II
      )
    • Glutamine amidotransferase PurL
    • Phosphoribosylformylglycinamidine synthase subunit II

Gene names

    • Name
      purL
    • Ordered locus names
      NWMN_0937

Organism names

Accessions

  • Primary accession
    A6QFS7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000723001-729Phosphoribosylformylglycinamidine synthase subunit PurL

Interaction

Subunit

Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.

Structure

Family & Domains

Sequence similarities

Belongs to the FGAMS family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    729
  • Mass (Da)
    79,536
  • Last updated
    2007-08-21 v1
  • MD5 Checksum
    9809747F8AD60A8048233A9C20708600
MSKFIEPSVEEIKLEKVYQDMGLSDQEYEKVCDILGRQPNFTETGIFSVMWSEHCSYKHSKPFLKQFPTSGDHVLMGPGEGAGVVDIGDNQAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIVSIGARPINLLNSLRFGELDNKQNQRLLKGVVKGIGGYGNCIGIPTTAGEIEFDERYDGNPLVNAMCVGVINHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEELTEESESKRPSVQIGDPFVGKKLMEATLEAITFDELVGIQDMGAAGLTSSSSEMAAKGGSGLHLRLEQVPTREPGISPYEMMLSETQERMLLVVEKGTEQKFLDLFDKHELDSAVIGEVTDTNRFVLTYDDEVYADIPVEPLADEAPVYILEGEEKDYNTSKNDYTHIDVKDTFFKLLKHPTIASKHYLYDQYDQQVGANTIIKPGLQASVVRVEGTNKAIASTIDGEARYVYNNPYEGGKMVVAEAYRNLIAVGATPLAMTDCLNYGSPEKKEIYQQLIDSTKGMAEACDILKTPVVSGNVSLYNETKGTSIFPTPVVGMVGLIENVNYLNDFEPQVGDKLYLIGDTKDDFGGSQLEKLIYGKVNHEFESLDLSSEVEKGESIKTAIREGLLSHVQTVGKGGLLITLAKLSAHYGLGLKSSIDITNAQLFSETQGRYVVSVKSGKTLNIDNAIEIGLLTDSDNFKVTTPYTEISENVSDIKQIWEGAIAQCLTTQD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009351
EMBL· GenBank· DDBJ
BAF67209.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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