A0A7X1F537 · A0A7X1F537_9SPHN

  • 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 site45
Binding site48ATP (UniProtKB | ChEBI)
Binding site87ATP (UniProtKB | ChEBI)
Binding site89Mg2+ 1 (UniProtKB | ChEBI)
Binding site90-93substrate
Active site91Proton acceptor
Binding site112substrate
Binding site113Mg2+ 2 (UniProtKB | ChEBI)
Binding site236substrate
Binding site264Mg2+ 2 (UniProtKB | ChEBI)
Binding site308-310substrate
Binding site497ATP (UniProtKB | ChEBI)
Binding site534ATP (UniProtKB | ChEBI)
Binding site535Mg2+ 1 (UniProtKB | ChEBI)
Binding site537substrate

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
      H7F49_02465

Organism names

  • Taxonomic identifier
  • Strain
    • 4Y4
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Novosphingobium

Accessions

  • Primary accession
    A0A7X1F537

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
Domain12-49Phosphoribosylformylglycinamidine synthase linker
Domain70-185PurM-like N-terminal
Domain198-347PurM-like C-terminal
Domain440-563PurM-like N-terminal
Domain577-699PurM-like C-terminal

Sequence similarities

Belongs to the FGAMS family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    731
  • Mass (Da)
    77,838
  • Last updated
    2021-06-02 v1
  • MD5 Checksum
    CA2201C9E7E6193FE3CD77509E19A8ED
MSQITPDVVAAHGLSEEEYARVLHALGREPNLVELGIFSVMWSEHCSYKSSRIHLKKLPTEAPWVICGPGENAGVIDIGDGQAAIFKMESHNHPSYIEPYQGAATGVGGILRDVFTMGARPVANMNALRFGRPDHPKMKHLVQGVVAGIGGYGNCVGVPTVGGETNFHRAYDGNILVNAMTVGVADQDKIFYSAATGIGNPIVYVGSKTGRDGIHGATMASADFDEKSEEKRPTVQVGDPFTEKLLIEACLELMATDAIVAIQDMGAAGLTSSSVEMASKGGAGIRLNMNRVPCREEGMTPYEMMLSESQERMLMVLKPGKEAMAEAIFRKWELDFAVIGEVTEAQADGGHMVLEFDGEVVCDIPLGPLADDAPLYDRPHVSLDEYKAWAKVAPLDQVPASSDLGADLLKLIGCPDLASRRWIYEQYDSQVGADTMQKSGGDAAVVRVHGTTKALAISTDCTPRYCYADPYEGGKQAVVETWRNICAVGARPLAITNCLNFANPQRPEIMAQIVEALRGMGDACRALDYPIVSGNVSLYNESKATGGGSAILPTPAIGGVGLMEDHSVMATVPFKAAGEAIFVIGQSNGHLGQSLWLRELHGREDGAPPPVDLAAERCHGEFVRQLIAEGKVSAVHDVSDGGLLMALAEMAMASGIGCTLEDIGDHFTAFGEDQGRYVVTSAVADQIQAAGIPMTRIGTTGGDSLRGPGFTVSIAALKAEHERFFKAWMEA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACLAU010000002
EMBL· GenBank· DDBJ
MBC2650562.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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