A0A125RA93 · A0A125RA93_9EURY

  • Protein
    Phosphoribosylformylglycinamidine synthase subunit PurL
  • Gene
    purL
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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 site34
Binding site37ATP (UniProtKB | ChEBI)
Binding site78Mg2+ 1 (UniProtKB | ChEBI)
Binding site79-82substrate
Active site80Proton acceptor
Binding site101substrate
Binding site102Mg2+ 2 (UniProtKB | ChEBI)
Binding site226substrate
Binding site254Mg2+ 2 (UniProtKB | ChEBI)
Binding site298-300substrate
Binding site474ATP (UniProtKB | ChEBI)
Binding site511ATP (UniProtKB | ChEBI)
Binding site512Mg2+ 1 (UniProtKB | ChEBI)
Binding site514substrate

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
    • ORF names
      TL18_00410

Organism names

  • Taxonomic identifier
  • Strain
    • YE315
  • Taxonomic lineage
    Archaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanobrevibacter

Accessions

  • Primary accession
    A0A125RA93

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

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

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-38Phosphoribosylformylglycinamidine synthase linker
Domain59-174PurM-like N-terminal
Domain187-339PurM-like C-terminal
Domain418-535PurM-like N-terminal
Domain549-685PurM-like C-terminal

Sequence similarities

Belongs to the FGAMS family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    712
  • Mass (Da)
    77,260
  • Last updated
    2016-04-13 v1
  • Checksum
    A47C8C8B6F4FE862
MTLADSEIEYIEGILGRKMNELEEGMLDVMFSEHCSYKSSRPFLRAFPTEGENIILGPGDDAGLVSVTDKYALAVGMESHNHPSAIEPYGGAGTGIGGILRDIISMGAMPIALLDSLRFGPLEDEKSRYLFEHVVKGISDYGNRVGVPTVAGEIEFDESFRTNPLVNVMCVGLVEKDKIVRAEAPNIGDVFLLMGGTTGRDGIHGVTFASEELTSDSETEDRPAVQVADPFTKKRVLEASLEILEKINVSGVKDLGGGGLTCCISELVDSSSNGALVDLRAIPLRETGMTPYEIMLSESQERMVFVINPDDVELAKQICDKHEIASSIIGEVIEGNNMIISDEGEEIANLPTILLADPPSIDRPICEIPEDTEKIELKEPGVYESLPKLLASPNIASKEWVYKQYDHEVQVRTVVKPGDDAAVLRIDENTAIALTTDSNTIHTKLSPFDGAAGCVAEAIRNVISMGATPYAVVDCLNFGNPETPEILWQFKTAIEGMSLVAEKFDAPVISGNVSFYNETEGIKINPTPAVGVIGVENIENIRTMDFKNEGDKIILIGKTYDELTGSEYQRTIHNIEKGTAPRIRIDDEVANGQTVLKLIDDDADKNITAVHDVSAGGLAVALSEMVIKSGLGCEVELKDDELDKIQLLYSESHGRYILTVKADALDDVLSQIDVDVCVIGEVKGDSLIVNGHEFSFEDLDNAYHGVIEQYMA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP010834
EMBL· GenBank· DDBJ
AMD16633.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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