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Protein

Adenylosuccinate synthetase

Gene

ADE12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.2 Publications

Catalytic activityi

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Enzyme regulationi

Inhibited by GMP. Inhibited by chloride. Inhibited in a highly specific manner by the binding of a 44-base DNA oligonucleotide carrying the ARS core consensus sequence.1 Publication

Kineticsi

  1. KM=1650 µM for L-aspartate2 Publications
  2. KM=200 µM for IMP2 Publications
  3. KM=1650 µM for GTP2 Publications

    pH dependencei

    Optimum pH is 8.0.2 Publications

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.2 Publications

    Pathway: AMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes AMP from IMP.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Adenylosuccinate synthetase (ADE12)
    2. Adenylosuccinate lyase (ADE13)
    This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei12 – 121Proton acceptorUniRule annotation
    Metal bindingi12 – 121MagnesiumUniRule annotation
    Metal bindingi39 – 391Magnesium; via carbonyl oxygenUniRule annotation
    Active sitei40 – 401Proton donorUniRule annotation
    Binding sitei134 – 1341IMPUniRule annotation
    Binding sitei148 – 1481IMP; shared with dimeric partnerUniRule annotation
    Binding sitei230 – 2301IMPUniRule annotation
    Binding sitei245 – 2451IMPUniRule annotation
    Binding sitei309 – 3091IMPUniRule annotation
    Binding sitei311 – 3111GTPUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 177GTPUniRule annotation
    Nucleotide bindingi39 – 413GTPUniRule annotation
    Nucleotide bindingi337 – 3393GTPUniRule annotation
    Nucleotide bindingi419 – 4213GTPUniRule annotation

    GO - Molecular functioni

    • adenylosuccinate synthase activity Source: SGD
    • DNA replication origin binding Source: SGD
    • GTP binding Source: UniProtKB-HAMAP
    • magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    • 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
    • purine nucleotide biosynthetic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-509.
    YEAST:YNL220W-MONOMER.
    ReactomeiREACT_301060. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00075; UER00335.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylosuccinate synthetaseUniRule annotation (EC:6.3.4.4UniRule annotation)
    Short name:
    AMPSaseUniRule annotation
    Short name:
    AS-synthetase
    Short name:
    AdSSUniRule annotation
    Alternative name(s):
    IMP--aspartate ligaseUniRule annotation
    Gene namesi
    Name:ADE12UniRule annotation
    Ordered Locus Names:YNL220W
    ORF Names:N1290
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XIV

    Organism-specific databases

    EuPathDBiFungiDB:YNL220W.
    SGDiS000005164. ADE12.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 433432Adenylosuccinate synthetasePRO_0000095138Add
    BLAST

    Proteomic databases

    MaxQBiP80210.
    PaxDbiP80210.
    PeptideAtlasiP80210.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRP40P332032EBI-14267,EBI-701
    RSP5P399402EBI-14267,EBI-16219

    Protein-protein interaction databases

    BioGridi35616. 27 interactions.
    DIPiDIP-4286N.
    IntActiP80210. 8 interactions.
    MINTiMINT-560386.
    STRINGi4932.YNL220W.

    Structurei

    3D structure databases

    ProteinModelPortaliP80210.
    SMRiP80210. Positions 2-429.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni12 – 154IMP bindingUniRule annotation
    Regioni37 – 404IMP bindingUniRule annotation
    Regioni305 – 3117Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the adenylosuccinate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0104.
    GeneTreeiENSGT00390000015553.
    HOGENOMiHOG000260959.
    InParanoidiP80210.
    KOiK01939.
    OMAiRCGIIEE.
    OrthoDBiEOG7B5X59.

    Family and domain databases

    HAMAPiMF_00011. Adenylosucc_synth.
    InterProiIPR018220. Adenylosuccinate_synthase_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11846. PTHR11846. 1 hit.
    PfamiPF00709. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SMARTiSM00788. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00184. purA. 1 hit.
    PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
    PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P80210-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVNVVLGSQW GDEGKGKLVD LLVGKYDIVA RCAGGNNAGH TIVVDGVKYD
    60 70 80 90 100
    FHMLPSGLVN PNCQNLLGNG VVIHVPSFFK ELETLEAKGL KNARSRLFVS
    110 120 130 140 150
    SRAHLVFDFH QVTDKLRELE LSGRSKDGKN IGTTGKGIGP TYSTKASRSG
    160 170 180 190 200
    LRVHHLVNDQ PGAWEEFVAR YKRLLETRRQ RYGDFEYDFE AKLAEYKKLR
    210 220 230 240 250
    EQLKPFVVDS VVFMHNAIEA KKKILVEGAN ALMLDIDFGT YPYVTSSNTG
    260 270 280 290 300
    IGGVLTGLGI PPRTIDEIYG VVKAYTTRVG EGPFPTEQLN ENGEKLQTIG
    310 320 330 340 350
    AEFGVTTGRK RRCGWLDLVV LKYSTLINGY TSLNITKLDV LDTFKEIPVG
    360 370 380 390 400
    ISYSIQGKKL DLFPEDLNIL GKVEVEYKVL PGWDQDITKI TKYEDLPENA
    410 420 430
    KKYLKYIEDF VGVPVEWVGT GPARESMLHK EIK
    Length:433
    Mass (Da):48,279
    Last modified:January 23, 2007 - v3
    Checksum:i800E0F4062D9856F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2371D → G AA sequence (PubMed:8376380).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L22185 Genomic DNA. Translation: AAA91338.1.
    Z48671 Genomic DNA. Translation: CAA88590.1.
    Z71496 Genomic DNA. Translation: CAA96123.1.
    BK006947 Genomic DNA. Translation: DAA10336.1.
    PIRiS48515.
    RefSeqiNP_014179.1. NM_001183058.1.

    Genome annotation databases

    EnsemblFungiiYNL220W; YNL220W; YNL220W.
    GeneIDi855501.
    KEGGisce:YNL220W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L22185 Genomic DNA. Translation: AAA91338.1.
    Z48671 Genomic DNA. Translation: CAA88590.1.
    Z71496 Genomic DNA. Translation: CAA96123.1.
    BK006947 Genomic DNA. Translation: DAA10336.1.
    PIRiS48515.
    RefSeqiNP_014179.1. NM_001183058.1.

    3D structure databases

    ProteinModelPortaliP80210.
    SMRiP80210. Positions 2-429.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35616. 27 interactions.
    DIPiDIP-4286N.
    IntActiP80210. 8 interactions.
    MINTiMINT-560386.
    STRINGi4932.YNL220W.

    Proteomic databases

    MaxQBiP80210.
    PaxDbiP80210.
    PeptideAtlasiP80210.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYNL220W; YNL220W; YNL220W.
    GeneIDi855501.
    KEGGisce:YNL220W.

    Organism-specific databases

    EuPathDBiFungiDB:YNL220W.
    SGDiS000005164. ADE12.

    Phylogenomic databases

    eggNOGiCOG0104.
    GeneTreeiENSGT00390000015553.
    HOGENOMiHOG000260959.
    InParanoidiP80210.
    KOiK01939.
    OMAiRCGIIEE.
    OrthoDBiEOG7B5X59.

    Enzyme and pathway databases

    UniPathwayiUPA00075; UER00335.
    BioCyciMetaCyc:MONOMER-509.
    YEAST:YNL220W-MONOMER.
    ReactomeiREACT_301060. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    NextBioi979499.
    PROiP80210.

    Family and domain databases

    HAMAPiMF_00011. Adenylosucc_synth.
    InterProiIPR018220. Adenylosuccinate_synthase_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11846. PTHR11846. 1 hit.
    PfamiPF00709. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SMARTiSM00788. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00184. purA. 1 hit.
    PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
    PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Saccharomyces cerevisiae ADE12 gene, coding for adenylosuccinate synthetase (EC 6.3.4.4). Cloning, sequencing, expression, and superproduction."
      Andreichuk I.V., Shabes A.V., Ryzhova T.A., Kotova I.A., Domkin V.D.
      Mol. Genet. Mikrobiol. Virusol. 1:21-28(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Enzymatic properties and inhibition by single-stranded autonomously replicating sequences of adenylosuccinate synthase from Saccharomyces cerevisiae."
      Gallert K.C., Ohanjan T., Daignan-Fornier B., Lottspeich F., Krauss G.
      Eur. J. Biochem. 239:487-493(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INHIBITION BY SS-DNA, SUBUNIT.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Characterization of two novel single-stranded DNA-specific autonomously replicating sequence-binding proteins from Saccharomyces cerevisiae, one of which is adenylosuccinate synthetase."
      Zeidler R., Hobert O., Johannes L., Faulhammer H., Krauss G.
      J. Biol. Chem. 268:20191-20197(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-23 AND 234-245.
    6. "Adenylosuccinate synthase from Saccharomyces cerevisiae: homologous overexpression, purification and characterization of the recombinant protein."
      Lipps G., Krauss G.
      Biochem. J. 341:537-543(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION.
    7. "Adenylosuccinate synthetase of the yeast Saccharomyces cerevisiae: purification and properties."
      Ryzhova T.A., Andreichuk Y.V., Domkin V.D.
      Biochemistry (Mosc.) 63:650-656(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPURA_YEAST
    AccessioniPrimary (citable) accession number: P80210
    Secondary accession number(s): D6W0X0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 141 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 56800 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.