B2JGM6 · B2JGM6_PARP8

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 site325-336ATP (UniProtKB | ChEBI)
Binding site714ATP (UniProtKB | ChEBI)
Binding site715Mg2+ (UniProtKB | ChEBI)
Binding site754Mg2+ (UniProtKB | ChEBI)
Binding site758Mg2+ (UniProtKB | ChEBI)
Binding site924Mg2+ (UniProtKB | ChEBI)
Binding site926ATP (UniProtKB | ChEBI)
Active site1199Nucleophile
Active site1320
Active site1322

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
      Bphy_1022

Organism names

Accessions

  • Primary accession
    B2JGM6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain38-162Phosphoribosylformylglycinamidine synthase N-terminal
Domain183-232Phosphoribosylformylglycinamidine synthase linker
Domain464-621PurM-like C-terminal
Domain876-1021PurM-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
    1,359
  • Mass (Da)
    147,028
  • Last updated
    2008-06-10 v1
  • Checksum
    327E02AFEB2EEF2E
MAHFSCFPGASALSDFRQTRLLDTLSRIDASIVGVRGQYLHFVNSQTPLSSEDSAKIEALMHYGDPFDAGKDKGAAETFLVVPRFGTVSPWASKATDIAHHCGLAHVRRIERGVEYTVVLKGGLLGGKKALSEAARAAVVAALHDRMTESVAPSRDHAMHLFDELPAKPLQTVGVLTDGRQALEKANSELGLALADDEIDYLADAFTKLGRNPTDVELMMFAQANSEHCRHKIFNASWTIDGETQDMSLFNMIRNTEKLNPQGTIVAYSDNSSIMQGGMAERWFPRKPAHADELGERYGRHTELTHTLMKVETHNHPTAISPFPGAATGAGGEIRDEGATGRGARPKAGLTGFTVSNLELPDAREPWENARDANQPVGHRNAADQFATYGRPDRIASPLQIMIDGPLGGAAFNNEFGRPNLGGYFRTYEQNVAGRVRGYHKPIMIAGGLGNVSDQHTHKHDLPAGSLLIQIGGPGMRIGMGGGAASSMATGTNTAELDFDSVQRGNPEIERRAQEVINSCWQLGEGNPILSIHDVGAGGLSNAFPELVDGADKGALFELRKIQLEESGLSPREIWSNEAQERYVLAIPPTRLEEFAAICERERCPFAVVGAATAERQLKLIDADKADGSAHEPVDMPMEVLLGKPPRMHRDVKRESTPLQPVDVTHIALHEAAVNVLRHPTVASKSFLITIGDRSVGGTTARDQMVGPWQVPVADCAITTVDYAGFRGEAMTMAERTPLAVIDAPASGRMAVGEAVTNIASAPIASLDKLKLSANWMAACGSPGEDAALYDTVKAIGMELCPALGIGIPVGKDSLSMRTKWADGNVEKEVVAPVSLIISAFAPVEDVRRHLTPQLMSVREAGETVLIAIDLGRGKQRLGGSILAQVTQQVGDTVPDVDDAEDLKRFFAAIQALNADGKLLAYHDRSDGGLWTTVCEMAFAGHVGVSLNVDMLTLDPDHEFDYGDAKDWTKQTSGRREDRTIRALFNEELGAVVQVRAADRDAVLAALREHGLSACSHVIGKPNTNDMIEIYRDAKKIFDAPRAELHRTWSEVSWRIARLRDNPACADAEFEMLLDTADPGMQPHLSFDPVEDVAAPFVGKGARPRVAILREQGVNSHLETAYAFDRAGFDAHDVHMSDLLSGRATLADFAGAVACGGFSYGDVLGAGEGWAKTIRFNAQLADMFAAFFGRSDTFALGICNGCQMMSSLASMIPGADAWPKFTRNKSEKFEARFSLVEVQSSPSIFFAGMESSRIPVAVAHGEGFADFSQQGDASRVAVALRYVDHRGQPTEQYPFNPNGSPAGITSVTTPDGRFTVLMPHTERVHRNVQMSWHPQAWKESATDGSPWMRVFQNARKWLG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001043
EMBL· GenBank· DDBJ
ACC70211.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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