P38972 · PUR4_YEAST

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 (By similarity).

Miscellaneous

Present with 40800 molecules/cell in log phase SD medium.

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 site345-356ATP (UniProtKB | ChEBI)
Binding site424-426ATP (UniProtKB | ChEBI)
Binding site719ATP (UniProtKB | ChEBI)
Binding site720Mg2+ (UniProtKB | ChEBI)
Binding site762Mg2+ (UniProtKB | ChEBI)
Binding site766Mg2+ (UniProtKB | ChEBI)
Binding site930Mg2+ (UniProtKB | ChEBI)
Binding site932ATP (UniProtKB | ChEBI)
Active site1187Nucleophile
Active site1319
Active site1321

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
Biological Processpurine nucleotide biosynthetic process

Keywords

Enzyme and pathway 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)
    • Formylglycinamide ribotide amidotransferase

Gene names

    • Name
      ADE6
    • Ordered locus names
      YGR061C

Organism names

Accessions

  • Primary accession
    P38972
  • Secondary accessions
    • D6VUJ6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylthreonine
ChainPRO_00001004052-1358Phosphoribosylformylglycinamidine synthase

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region339-363Disordered
Domain1093-1358Glutamine amidotransferase type-1

Sequence similarities

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,358
  • Mass (Da)
    148,905
  • Last updated
    1996-10-01 v2
  • Checksum
    A48A24ECB1BE7973
MTDYILPGPKALSQFRVDNLIKDINSYTNSTSVINELRSCYIHYVNGIAQNLSEQDTKLLEVLLTYDSALDIANDPLARQLNDAVANNLPSSALGEDTYLIRVVPRSGTISPWSSKATNIAHVCGLQDKVQRIERGLALLIKTVPGFPLLENLNDISLKCVYDRMTQQLYLTEPPNTMSIFTHEEPKPLVHVPLTPKDTKQSPKDILSKANTELGLALDSGEMEYLIHAFVETMKRDPTDVELFMFAQVNSEHCRHKIFNADWTIDGIKQQFTLFQMIRNTHKLNPEYTISAYSDNAAVLDSENDAFFFAPNSTTKEWTSTKERIPLLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGNEQPWELNIGKPYHIASALDIMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVLNHQGKEEIRGFHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIGLGGGAASSVASGEGSADLDFASVQRGNPEMERRCQQVIDACVALGNNNPIQSIHDVGAGGLSNALPELVHDNDLGAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVEDPLLKTTPIDLEMPILFGKPPKMSRETITEALNLPEANLSEIPSLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVTGTSLGETIISTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLNHIKLSANWMSPASHQGEGSKLYEAVQALGLDLCPALGVAIPVGKDSMSMKMKWDDKEVTAPLSLNITAFAPVFNTSKTWTPLLNRNTDDSVLVLVDLSAKQETKSLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLHQQKEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINIDGGDLESQLTNLFNEELGAVFQISAKNLSKFEKILNENGVAKEYISIVGKPSFQSQEIKIINSTTNDVIYANSRSELEQTWSKTSYEMQKLRDNPKTAEEEFASITDDRDPGLQYALTYNPADDMKIGLELSSQRPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRSQFSKFFNERQDTFAFGACNGCQFLSRLKDIIPGCENWPSFERNVSEQYEARVCMVQISQEKDNSSEESVFLNGMAGSKLPIAVAHGEGKATFSKSAEQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANSWYPEGKYEEWGGYGPWIRLFRSARRWVG

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict84in Ref. 1; AAA50357
Sequence conflict219-220in Ref. 1; AAA50357
Sequence conflict226in Ref. 1; AAA50357
Sequence conflict492in Ref. 1; AAA50357
Sequence conflict499in Ref. 1; AAA50357
Sequence conflict551in Ref. 1; AAA50357
Sequence conflict604in Ref. 1; AAA50357
Sequence conflict1169-1170in Ref. 1; AAA50357
Sequence conflict1298in Ref. 1; AAA50357

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U14566
EMBL· GenBank· DDBJ
AAA50357.1
EMBL· GenBank· DDBJ
Genomic DNA
Z72846
EMBL· GenBank· DDBJ
CAA97063.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006941
EMBL· GenBank· DDBJ
DAA08157.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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