A2SGN1 · A2SGN1_METPP

Function

function

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.

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 binding site, active site.

TypeIDPosition(s)Description
Binding site319-330ATP (UniProtKB | ChEBI)
Binding site695ATP (UniProtKB | ChEBI)
Binding site696Mg2+ (UniProtKB | ChEBI)
Binding site735Mg2+ (UniProtKB | ChEBI)
Binding site739Mg2+ (UniProtKB | ChEBI)
Binding site902Mg2+ (UniProtKB | ChEBI)
Binding site904ATP (UniProtKB | ChEBI)
Active site1180Nucleophile
Active site1301
Active site1303

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionphosphoribosylformylglycinamidine synthase activity
Biological Process'de novo' IMP biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoribosylformylglycinamidine synthase
  • EC number
  • Short names
    FGAM synthase
    ; FGAMS
  • Alternative names
    • Formylglycinamide ribonucleotide amidotransferase
      (FGAR amidotransferase
      ; FGAR-AT
      )

Gene names

    • Name
      purL
    • Ordered locus names
      Mpe_A1761

Organism names

Accessions

  • Primary accession
    A2SGN1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain41-160Phosphoribosylformylglycinamidine synthase N-terminal
Domain181-230Phosphoribosylformylglycinamidine synthase linker
Domain445-596PurM-like C-terminal
Domain845-1012PurM-like C-terminal

Sequence similarities

In the N-terminal section; belongs to the FGAMS family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,336
  • Mass (Da)
    142,937
  • Last updated
    2007-03-06 v1
  • Checksum
    E302F7EF41C8EA6F
MTQPTILSFDGGNALSAFRAQALLPRLQALAAGITAVHARHVHWVAAEAALDAAARDKLAGLLRYGNAYAGPTEGTLVLVMPRLGTVSPWASKATDIAHNCGLGIRRVERVTEYRLTLKGGLLGGSKPLTDAERAAVAELLHDRMTESVAFEHGAAAHLFDAQPGKPMETVDVIGRGRTALEAANRDFGLALSDDEIDYLVAAFTGLQRNPTDVELMMFAQANSEHCRHKIFNAQFTIDGEAQEHSMFQMIRHTHKTSPQHTIVAYSDNAAVMEGFPIERWLPQGYTNAPVYAARHETAHVLMKVETHNHPTAISPFAGASTGAGGEIRDEGATGRGARPKAGLTGFSVSNLQLPGTHEPWERVRYGKPEHIASALQIMIDGPLGGAAFNNEFGRPNLGGYFRVYEQTVGAGAQAQRRGYHKPIMIAGGLGTISDGQTHKIPFPAGTLLIQLGGPGMRIGMGGGAASSMAAGANTAALDFDSVQRGNPEIQRRAQEVLNHCWALGAGNPILAVHDVGAGGISNAFPELVHDAGRGARFDLRKVPLEESGLAPKEIWCNESQERYVLAIAPESLPLFEAMATRERCPYAVVGVASDALQLVLEDGPGGQGEHGTPIDMPMDVLLGKPPKMHRQVQRVAHHLEPLALAGVTLQQAAFDVLRHPTVASKRFLITIGDRTVGGLSHRDQMVGPWQVPVADCAVTLADHAGFHGEAMAMGERTPLALIDAPAAGRMAVAESITNLLAAPIELPRVKLSCNWMAACGEPGEDAALYDTVRAVGLELCPALGIAVPVGKDSLSMRTRWSDAESGEAKQVTAPVSLIVTAFASLADVRGTLTPQLQPGDTSLILIDLGQGRNRLGGSILAQTLEQLGDSAPDLDDAALLKQLVAAIHRLRGEGRLLAYHDRSDGGLWATVCEMAFAGHCGVSLNVDLLVTEGDGVSDSRMDSGDAKNWAGQVGARREELTLKALFAEELGAVIQVAGAERDKVLHVLREAGLGRHSHVIGKPNDRGVVEVWRDAKAVFSAPLRELHQAWDEVSWRIAALRDHPGCAEAEHAAAGAPDDAGLQWQPSFDPAEDVAAPFLKLARPKLAILREQGVNSHIEMAYAMAQAGFETYDVHMSDLQSGRARLDMYRGFVACGGFSYGDTLGAGEGWARSVLFNPRLADQFAAFFNRDDSFALGVCNGCQMMAALAPIIPGAQAWPKFTRNRSEQFEARLAQVEVLESPSLFFAGMAGSRLPIAVAHGEGYADFSQRGDARAVHRAMRYVDPAGRATEAYPHNPNGSPEGLTAVTTPDGRYTALMPHPERVFRNVQMSWSGGDVTAASPWLRMFRNARRWAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000555
EMBL· GenBank· DDBJ
ABM94720.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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