A0A014P7B6 · A0A014P7B6_9ACTN

  • 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.

TypeIDPosition(s)Description
Active site55
Binding site58ATP (UniProtKB | ChEBI)
Binding site100ATP (UniProtKB | ChEBI)
Binding site102Mg2+ 1 (UniProtKB | ChEBI)
Binding site103-106substrate
Active site104Proton acceptor
Binding site125substrate
Binding site126Mg2+ 2 (UniProtKB | ChEBI)
Binding site250substrate
Binding site278Mg2+ 2 (UniProtKB | ChEBI)
Binding site322-324substrate
Binding site510ATP (UniProtKB | ChEBI)
Binding site547ATP (UniProtKB | ChEBI)
Binding site548Mg2+ 1 (UniProtKB | ChEBI)
Binding site550substrate

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
      Z951_17390

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PRh5
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A014P7B6

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
Domain20-59Phosphoribosylformylglycinamidine synthase linker
Domain83-198PurM-like N-terminal
Domain211-366PurM-like C-terminal
Domain453-572PurM-like N-terminal
Domain585-721PurM-like C-terminal

Sequence similarities

Belongs to the FGAMS family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    749
  • Mass (Da)
    79,717
  • Last updated
    2014-06-11 v1
  • Checksum
    22573B9F4D24E4F6
MTLDTTKHAAQTPEAEQPWAELGLKQDEYERVRAILGRRPTGAELAMYSVMWSEHCSYKSSKVHLRQFGEKAPESDALLVGIGENAGVVDVGQGYAVTFKVESHNHPSYIEPYQGAATGVGGIVRDILAMGARPVAVMDPLRFGAADHPDTKRVLPGVVAGIGGYGNCLGLPNIGGEVVFDPCYQGNPLVNALCVGVMKHEDIHLAKASGTGNKVILYGARTGGDGIGGVSVLASETFDDSKPTKRPAVQVGDPFQEKLLIECTLEVFKEDLVEGIQDLGGAGLSCATSELASAGSGGMRVELDTVPLRDSSLSPEEILMSESQERMCAIVKPEKVDRFLEICEKWDVIATVIGEVTDGERLEIYWHGEQIVDVPPRTVAHEGPVYERPYARPEWQDALQADDAGKLPRPATAEELREQVLKVIGSPNQSSKSWITDQYDRFVQGNTVLAQPEDSGMVRVDEETGLGVAVATDGNGRYAKLDPYAGAQLALAESYRNVAASGAKPLAISNCLNFGSPEDPAVMWQFAEATRGLADGCLTLGTPVTGGNVSLYNQTGEVAIHPTPVVAVLGVIDDVARRTPIAFAEEGQLLYLLGDTAEELGGSAWSQVIHDHLGGLPPKVDLERERLLAEILISASRDGMVDAAHDLSDGGLIQALAESCLRGGKGARIVVPDGLDPFVLLFSESAGRAIVAVPRSEEVRFNDMCGARGLPAARIGVVDGDAIDVQGQFSIPLAELRESYEATIPGLLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABQ01000022
EMBL· GenBank· DDBJ
EXU66922.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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