A0A853MCG1 · A0A853MCG1_9CYAN

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 site47
Binding site50ATP (UniProtKB | ChEBI)
Binding site89ATP (UniProtKB | ChEBI)
Binding site91Mg2+ 1 (UniProtKB | ChEBI)
Binding site92-95substrate
Active site93Proton acceptor
Binding site114substrate
Binding site115Mg2+ 2 (UniProtKB | ChEBI)
Binding site238substrate
Binding site266Mg2+ 2 (UniProtKB | ChEBI)
Binding site310-312substrate
Binding site516ATP (UniProtKB | ChEBI)
Binding site553ATP (UniProtKB | ChEBI)
Binding site554Mg2+ 1 (UniProtKB | ChEBI)
Binding site556substrate

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
      A9P98_09575

Organism names

Accessions

  • Primary accession
    A0A853MCG1

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
Domain16-51Phosphoribosylformylglycinamidine synthase linker
Domain72-187PurM-like N-terminal
Domain200-351PurM-like C-terminal
Domain451-583PurM-like N-terminal
Domain597-739PurM-like C-terminal

Sequence similarities

Belongs to the FGAMS family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    778
  • Mass (Da)
    83,591
  • Last updated
    2021-09-29 v1
  • Checksum
    D3CC68276C1EF79F
MSTSPFSSQEIASQGIKPDEYADIVRRLGRHPNKAELGMFGVMWSEHCCYKNSRPLLKQFPTTGPRILVGPGENAGVVDLGQGLQLAFKIESHNHPSAVEPFQGAATGVGGILRDIFTMGARPIGILNSLRFGNLEDPKTQRLFTGVVSGIAHYGNCVGVPTVGGEVYFDSAYSGNPLVNVMALGLMETPTIVKSGAAGIGNPVLYVGSTTGRDGMGGASFASAELTDESMDNRPAVQVGDPFLEKSLIEACLEAFKTGAVVAAQDMGAAGITCSTSEMAAKGGVGIQFDLDKVPARELGMIPYEYLLSESQERMLFVSQKGREQELIDIFQRWGLHAVVAGEVISEPVVRILFQGEVAASIPAKALAENTPLYERKLLSEPPEYVKLAWEWTSAKLPTCDVRGIEVQGEFLSWQDILLKLLNTPTIASKSWVYRQYDHQVQNNTVLLPGGADAAVLRLRPLSESTVTHWESGVAATVDCNSRYVYLDPYEGAKAVVAEAARNLSCVGAQPLAVTDNLNFGSPEKEVGYWQLAYACKGISEGCKELGTPVTGGNVSLYNETFDAQGNPQAIYPTPVVGMVGLIEDLQKICGQGWQNVGDGIYLLGLPVSVKLELGGSEYLAVIHHTVAGKPPKINFALERDVQQACRYGISNKWVSSAHDSAEGGLIVALAECCLSGNLGASINLGISSNEECRFDEVLFGEGGARILVSVPGTYQQVWESYLQTHLGNNWQKLGSVVNLSSGLTVSTLDDYEVMGMDIPQMGNVYHQAIAQRLSFYE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LYXA01000001
EMBL· GenBank· DDBJ
OBU76529.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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