B0SB88 · PURL_LEPBA

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.

TypeIDPosition(s)Description
Active site47
Binding site50ATP (UniProtKB | ChEBI)
Binding site90ATP (UniProtKB | ChEBI)
Binding site92Mg2+ 1 (UniProtKB | ChEBI)
Binding site93-96substrate
Active site94Proton acceptor
Binding site115substrate
Binding site116Mg2+ 2 (UniProtKB | ChEBI)
Binding site240substrate
Binding site268Mg2+ 2 (UniProtKB | ChEBI)
Binding site312-314substrate
Binding site500ATP (UniProtKB | ChEBI)
Binding site537ATP (UniProtKB | ChEBI)
Binding site538Mg2+ 1 (UniProtKB | ChEBI)
Binding site540substrate

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
      LBF_2099

Organism names

Accessions

  • Primary accession
    B0SB88

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001948281-748Phosphoribosylformylglycinamidine 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
    748
  • Mass (Da)
    80,636
  • Last updated
    2008-04-08 v1
  • Checksum
    556B689019169365
MEKEKVSLADAKEHGLTETEFVEIQKILGRIPNSTELGIFSAMWSEHCSYKNSILKLKTLPTKSDKLLAGAGEENAGAMDIGDGLAVVFKIESHNHPTAVEPYQGAATGVGGIMRDIFTMGARPITSLNSLRFGDPKEPRNKYLLTRAVKGIGDYGNSLGIAVGGGELFLHPTFTKNPLVNAMTVGIAKHDEMASASTKGKVGNKVYIVGATTGRDGIHGASFASKDLTKESEEKRSAVQVGDPFMEKLLMEASLEAIQKKLLVGIQDMGAAGISCATSEMSAKGKTGMDVDLDKVPLREADMNAYEIMLSESQERMLVIPEVGKEGELVSIFHKWGLNAVEIGTVTADGILRIRKNGTLKAEIPAESLVLGGGAPRYVREEKRPTYLDEVVKFDPNKIPDLKPDTVPQTLNSLLSSLNISSRRPLYEQYDTEVGLVKVVEPGEDGGLVRIPGTKKGIAVATDCNSRYTYLNPYEGAQIAVCESARNVAATGAEPYGVTNNLNFGNPYIPENYYVFSECVRGLGDACRFLGLPVTGGNVSFYNESPEGPVFPTPTIGMVGVIDDVAKGLRTYPRTKEDVKYALVGNFQPTISASEYLYRSQGLDTGAIPNISLEKEKQTMDALIECRKNGLLTSAKDLSLGGLLVALAKIVIAGKKGVEVNLNELQTKVPRLDALCFGETGASFIVSFLPNDETKVRESFTSKGLSVYTLGSSSAKASLSVKGDGFHWEWTTKSLEVEFESGLKSYFE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000777
EMBL· GenBank· DDBJ
ABZ94594.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp