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P80210 (PURA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylosuccinate synthetase

Short name=AMPSase
Short name=AS-synthetase
Short name=AdSS
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase
Gene names
Name:ADE12
Ordered Locus Names:YNL220W
ORF Names:N1290
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP-Rule MF_03125

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_03125

Enzyme regulation

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. Ref.6

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_03125

Subunit structure

Homodimer. Ref.2 Ref.6 Ref.7

Subcellular location

Cytoplasm Ref.8.

Miscellaneous

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

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Biophysicochemical properties

Kinetic parameters:

KM=1650 µM for L-aspartate Ref.6 Ref.7

KM=200 µM for IMP

KM=1650 µM for GTP

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Optimum temperature is 35 degrees Celsius.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRP40P332032EBI-14267,EBI-701
RSP5P399402EBI-14267,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 433432Adenylosuccinate synthetase HAMAP-Rule MF_03125
PRO_0000095138

Regions

Nucleotide binding11 – 177GTP By similarity
Nucleotide binding39 – 413GTP By similarity
Nucleotide binding337 – 3393GTP By similarity
Nucleotide binding419 – 4213GTP By similarity
Region12 – 154IMP binding By similarity
Region37 – 404IMP binding By similarity
Region305 – 3117Substrate binding By similarity

Sites

Active site121Proton acceptor By similarity
Active site401Proton donor By similarity
Metal binding121Magnesium By similarity
Metal binding391Magnesium; via carbonyl oxygen By similarity
Binding site1341IMP By similarity
Binding site1481IMP; shared with dimeric partner By similarity
Binding site2301IMP By similarity
Binding site2451IMP By similarity
Binding site3091IMP By similarity
Binding site3111GTP By similarity

Experimental info

Sequence conflict2371D → G AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P80210 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 800E0F4062D9856F

FASTA43348,279
        10         20         30         40         50         60 
MVNVVLGSQW GDEGKGKLVD LLVGKYDIVA RCAGGNNAGH TIVVDGVKYD FHMLPSGLVN 

        70         80         90        100        110        120 
PNCQNLLGNG VVIHVPSFFK ELETLEAKGL KNARSRLFVS SRAHLVFDFH QVTDKLRELE 

       130        140        150        160        170        180 
LSGRSKDGKN IGTTGKGIGP TYSTKASRSG LRVHHLVNDQ PGAWEEFVAR YKRLLETRRQ 

       190        200        210        220        230        240 
RYGDFEYDFE AKLAEYKKLR EQLKPFVVDS VVFMHNAIEA KKKILVEGAN ALMLDIDFGT 

       250        260        270        280        290        300 
YPYVTSSNTG IGGVLTGLGI PPRTIDEIYG VVKAYTTRVG EGPFPTEQLN ENGEKLQTIG 

       310        320        330        340        350        360 
AEFGVTTGRK RRCGWLDLVV LKYSTLINGY TSLNITKLDV LDTFKEIPVG ISYSIQGKKL 

       370        380        390        400        410        420 
DLFPEDLNIL GKVEVEYKVL PGWDQDITKI TKYEDLPENA KKYLKYIEDF VGVPVEWVGT 

       430 
GPARESMLHK EIK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L22185 Genomic DNA. Translation: AAA91338.1.
Z48671 Genomic DNA. Translation: CAA88590.1.
Z71496 Genomic DNA. Translation: CAA96123.1.
BK006947 Genomic DNA. Translation: DAA10336.1.
PIRS48515.
RefSeqNP_014179.1. NM_001183058.1.

3D structure databases

ProteinModelPortalP80210.
SMRP80210. Positions 2-429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35616. 26 interactions.
DIPDIP-4286N.
IntActP80210. 8 interactions.
MINTMINT-560386.
STRING4932.YNL220W.

Proteomic databases

PaxDbP80210.
PeptideAtlasP80210.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL220W; YNL220W; YNL220W.
GeneID855501.
KEGGsce:YNL220W.

Organism-specific databases

SGDS000005164. ADE12.

Phylogenomic databases

eggNOGCOG0104.
GeneTreeENSGT00390000015553.
HOGENOMHOG000260959.
KOK01939.
OMADYVVRYQ.
OrthoDBEOG7B5X59.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-509.
YEAST:YNL220W-MONOMER.
UniPathwayUPA00075; UER00335.

Gene expression databases

GenevestigatorP80210.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11846. PTHR11846. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979499.
PROP80210.

Entry information

Entry namePURA_YEAST
AccessionPrimary (citable) accession number: P80210
Secondary accession number(s): D6W0X0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways