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UniProtKB/Swiss-Prot entry P80210


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PURA_YEAST
Primary accession number P80210
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 82)
Name and origin of the protein
Protein name Adenylosuccinate synthetase
Synonyms AdSS
EC 6.3.4.4
IMP--aspartate ligase
AMPSase
Gene name
Name: ADE12
OrderedLocusNames: YNL220W
ORFNames: N1290
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7603488 [NCBI, ExPASy, EBI, Israel, Japan]
Andreichuk I.V., Shabes A.V., Ryzhova T.A., Kotova I.A., Domkin V.D.;
"Saccharomyces cerevisiae ADE12 gene, coding for adenylosuccinate synthetase (EC 6.3.4.4). Cloning, sequencing, expression, and superproduction.";
Mol. Genet. Mikrobiol. Virusol. 1:21-28(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INHIBITION BY SS-DNA.
PubMed=8706758 [NCBI, ExPASy, EBI, Israel, Japan]
Gallert K.C., Ohanjan T., Daignan-Fornier B., Lottspeich F., Krauss G.;
"Enzymatic properties and inhibition by single-stranded autonomously replicating sequences of adenylosuccinate synthase from Saccharomyces cerevisiae.";
Eur. J. Biochem. 239:487-493(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
PROTEIN SEQUENCE OF 2-23 AND 234-245.
PubMed=8376380 [NCBI, ExPASy, EBI, Israel, Japan]
Zeidler R., Hobert O., Johannes L., Faulhammer H., Krauss G.;
"Characterization of two novel single-stranded DNA-specific autonomously replicating sequence-binding proteins from Saccharomyces cerevisiae, one of which is adenylosuccinate synthetase.";
J. Biol. Chem. 268:20191-20197(1993).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-143, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L22185; AAA91338.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z48671; CAA88590.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71496; CAA96123.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S48515; S48515.
RefSeq NP_014179.1; -.
3D structure databases
HSSP P28650; 1IWE. [HSSP ENTRY / PDB]
ModBase P80210.
Protein-protein interaction databases
DIP DIP:4286N; -.
IntAct P80210; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-509; -.
Organism-specific databases
CYGD YNL220w; -.
SGD S000005164; ADE12.
Yeast-GFP YNL220W.
Gene expression databases
ArrayExpress P80210; -.
GermOnline YNL220W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0004019; Molecular function: adenylosuccinate synthase activity (inferred from direct assay from SGD).
GO:0003688; Molecular function: DNA replication origin binding (inferred from direct assay from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0006164; Biological process: purine nucleotide biosynthetic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001114; AdlSucc_Synth.
Graphical view of domain structure.
PANTHER PTHR11846; Asucc_synthtase; 1.
Pfam PF00709; Adenylsucc_synt; 1.
Pfam graphical view of domain structure.
ProDom PD001188; Asucc_synthtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00788; Adenylsucc_synt; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00184; purA; 1.
PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1.
PS00513; ADENYLOSUCCIN_SYN_2; 1.
BLOCKS P80210.
Proteomic databases
PeptideAtlas P80210; -.
Genome annotation databases
Ensembl YNL220W; Saccharomyces cerevisiae. [Contig view]
GeneID 855501; -.
GenomeReviews Y13139_GR; YNL220W.
KEGG sce:YNL220W; -.
NMPDR fig|4932.3.peg.5244; -.
Phylogenomic databases
HOGENOM P80210; -.
Other
LinkHub P80210; -.
ProtoNet P80210.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; DNA-binding; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   433  432     Adenylosuccinate synthetase. PRO_0000095138
NP_BIND   11    17  7     GTP (By similarity). 
ACT_SITE   145   145        By similarity. 
ACT_SITE   152   152        By similarity. 
METAL   12    12        Magnesium (By similarity). 
METAL   39    39        Magnesium; via carbonyl oxygen (By similarity). 
MOD_RES   122   122        Phosphoserine. 
MOD_RES   143   143        Phosphoserine. 
CONFLICT   237   237        D -> G (in Ref. 4; AA sequence). 
Sequence information
Length: 433 AA [This is the length of the unprocessed precursor] Molecular weight: 48279 Da [This is the MW of the unprocessed precursor] CRC64: 800E0F4062D9856F [This is a checksum on the sequence]
        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 

P80210 in FASTA format

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