A0A9X4NFU7 · A0A9X4NFU7_9LACT

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

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 site275Mg2+ 2 (UniProtKB | ChEBI)
Binding site319-321substrate
Binding site504ATP (UniProtKB | ChEBI)
Binding site541ATP (UniProtKB | ChEBI)
Binding site542Mg2+ 1 (UniProtKB | ChEBI)
Binding site544substrate

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
      OGZ51_04160

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 3
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Lactococcus

Accessions

  • Primary accession
    A0A9X4NFU7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

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

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-58Phosphoribosylformylglycinamidine synthase linker
Domain79-194PurM-like N-terminal
Domain207-362PurM-like C-terminal
Domain447-566PurM-like N-terminal
Domain579-713PurM-like C-terminal

Sequence similarities

Belongs to the FGAMS family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    739
  • Mass (Da)
    79,598
  • Last updated
    2023-11-08 v1
  • Checksum
    523218446137623B
MTLEMSPEQIQESKIYREWGLTDEEYLKIKDEILDGRLPNFTETGMYAVMWSEHCCYKNSKPVLKKFPTTGPQVLMGPGEGAGVVDIGDDLAVVFKAESHNHPSYVEPYEGAATGSGGIIRDIFSMGARPIAILDSLRFGPIDSGKTRHIVDQVTAGIAGYGNCIGIPTVGGEVAFDESYAGNPLVNVMCVGLIEHKHIQKGQAKGVGNSIFYVGAKTGRDGIHGASFASKEFGSGSETQRSAVQVGDPFMEKLLLEACIEVIQNHGDILVGIQDMGAAGLVSSTSEMASKAGSGLRLNLDNVPQRETEMIPYEMMLSESQERMVLCVKKGHEQEIIDLFKKYDLDAVNIGQVTDDGFYTLYHKGEMVAHVPVDSLAEDAPTYYREAKVPERIQKFTDSEKYLPEITDSAVSEIFKKLLAQPTIASKKSIYETYDSRVMTNTVVAPGSDSAVLRVRGTNKALAMTTDCNARYLYLDPEKGGAIAVAEAARNIVASGGKPLAITDCLNFGNPEKPEQFWELTTAADGISRSCLALDTPVISGNVSLYNETNGSAILPTPMIGMVGLIENVKNITTQEFKKAGDLIVLVGQTFDDFSGSEIQKMLTGEISGRIDFDLETEKINQDFVLKAITDGLVSSAHDLAEGGLAVALAESAFANGLGVDVKVDLTNAQLFSETQGRFVLSISPENQAAFEKLLTESSVSGEVIGKVTDSGILEMNELSISTDEAVSIYEGALPALMK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAOWLY010000003
EMBL· GenBank· DDBJ
MDG4983340.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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