A0A3A1VUF4 · A0A3A1VUF4_STAAU

  • 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.

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 site273Mg2+ 2 (UniProtKB | ChEBI)
Binding site495ATP (UniProtKB | ChEBI)
Binding site532ATP (UniProtKB | ChEBI)
Binding site533Mg2+ 1 (UniProtKB | ChEBI)
Binding site535substrate

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
      DQU50_00960
      , DQU51_12930
      , G0Z31_07080
      , G6Y24_06020
      , GQX52_12005
      , GZ111_002950
      , M1K003_1631
      , SAMEA70153168_01576

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • M1K003
    • Pt013
    • pt013
    • Pt014
    • pt014
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    A0A3A1VUF4

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
Domain13-58Phosphoribosylformylglycinamidine synthase linker
Domain79-194PurM-like N-terminal
Domain207-361PurM-like C-terminal
Domain440-557PurM-like N-terminal

Sequence similarities

Belongs to the FGAMS family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    729
  • Mass (Da)
    79,563
  • Last updated
    2018-12-05 v1
  • Checksum
    B9C034B3161966FC
MSKFIEPSVEEIKLEKVYQDMGLSDQEYEKVCDILGRQPNFTETGIFSVMWSEHCSYKHSKPFLKQFPTSGEHVLMGPGEGAGVVDIGDNQAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIVSIGARPINLLNSLRFGELDNKQNQRLLKGVVKGIGGYGNCIGIPTTAGEIEFDERYDGNPLVNAMCVGVINHDMIQKGTAKGVGNSVIYVGLKTGRDGIHGATFASEELTEESESKRPSVQIGDPFVGKKLMEATLEAITFDELVGIQDMGAAGLTSSSSEMAAKGGSGLHLRLEQVPTREPGISPYEMMLSETQERMLLVVEKGNEQKFLDLFDKHELDSAVIGEVTDTNRFVLTYDDEVYADIPVEPLADEAPVYILEGEEKDYNTSKNDYTHIDVKDTFFKLLKHPTIASKHYLYDQYDQQVGANTIIKPGLQASVVRVEGTNKAIASTIDGEARYVYNNPYEGGKMVVAEAYRNLIAVGATPLAMTDCLNYGSPEKKEIYQQLIDSTKGMAEACDILKTPVVSGNVSLYNETKGTSIFPTPVVGMVGLIENVNYLNDFEPQVGDKLYLIGDTKDDFGGSQLEKLIYGKVNHEFESLDLSSEVEKGESIKTAIREGLLSHVQTVGKGGLLITLAKLSAHYGLGLKSSIDITNAQLFSETQGRYVVSVKSGKTLNIDNAIEIGLLTDSDNFKVTTPYTEISENVSDIKQIWEGAIAQCLTTQD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAIIGN010000005
EMBL· GenBank· DDBJ
CAC8237353.1
EMBL· GenBank· DDBJ
Genomic DNA
BDVT01000007
EMBL· GenBank· DDBJ
GBV20637.1
EMBL· GenBank· DDBJ
Genomic DNA
JAAJIY010000017
EMBL· GenBank· DDBJ
NGK21279.1
EMBL· GenBank· DDBJ
Genomic DNA
JAALTR010000170
EMBL· GenBank· DDBJ
NGW67053.1
EMBL· GenBank· DDBJ
Genomic DNA
JAANDN010000108
EMBL· GenBank· DDBJ
NUY69343.1
EMBL· GenBank· DDBJ
Genomic DNA
QNXH01000001
EMBL· GenBank· DDBJ
TXL38377.1
EMBL· GenBank· DDBJ
Genomic DNA
QNXF01000001
EMBL· GenBank· DDBJ
TXL47676.1
EMBL· GenBank· DDBJ
Genomic DNA
CP152420
EMBL· GenBank· DDBJ
XAJ30985.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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