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P80210

- PURA_YEAST

UniProt

P80210 - PURA_YEAST

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Protein

Adenylosuccinate synthetase

Gene

ADE12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 Mg(2+) 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

Pathwayi

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

  1. adenylosuccinate synthase activity Source: SGD
  2. DNA replication origin binding Source: SGD
  3. GTP binding Source: UniProtKB-HAMAP
  4. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
  2. 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_235398. 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: Chromosome XIV

Organism-specific databases

SGDiS000005164. ADE12.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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.

Expressioni

Gene expression databases

GenevestigatoriP80210.

Interactioni

Subunit structurei

Homodimer.3 PublicationsUniRule annotation

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.
OMAiYYMYEAL.
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 .
PIRi S48515.
RefSeqi NP_014179.1. NM_001183058.1.

3D structure databases

ProteinModelPortali P80210.
SMRi P80210. Positions 2-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35616. 27 interactions.
DIPi DIP-4286N.
IntActi P80210. 8 interactions.
MINTi MINT-560386.
STRINGi 4932.YNL220W.

Proteomic databases

MaxQBi P80210.
PaxDbi P80210.
PeptideAtlasi P80210.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL220W ; YNL220W ; YNL220W .
GeneIDi 855501.
KEGGi sce:YNL220W.

Organism-specific databases

SGDi S000005164. ADE12.

Phylogenomic databases

eggNOGi COG0104.
GeneTreei ENSGT00390000015553.
HOGENOMi HOG000260959.
InParanoidi P80210.
KOi K01939.
OMAi YYMYEAL.
OrthoDBi EOG7B5X59.

Enzyme and pathway databases

UniPathwayi UPA00075 ; UER00335 .
BioCyci MetaCyc:MONOMER-509.
YEAST:YNL220W-MONOMER.
Reactomei REACT_235398. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi 979499.
PROi P80210.

Gene expression databases

Genevestigatori P80210.

Family and domain databases

HAMAPi MF_00011. Adenylosucc_synth.
InterProi IPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11846. PTHR11846. 1 hit.
Pfami PF00709. Adenylsucc_synt. 1 hit.
[Graphical view ]
SMARTi SM00788. Adenylsucc_synt. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00184. purA. 1 hit.
PROSITEi PS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 137 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