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Sample Preparation and Post-separation Analysis Searching in 'SWISS-2DPAGE' for entry matching: P0A7D4 SWISS-2DPAGE:  P0A7D4 P0A7D4 General information about the entry View entry in simple text format Entry name PURA_ECOLI Primary accession number P0A7D4 Secondary accession number(s) P12283 integrated into SWISS-2DPAGE on  May 15, 2003 (release 16) 2D Annotations were last modified on May 15, 2003 (version 1) General Annotations were last modified on  May 19, 2011 (version 7) Name and origin of the protein Description RecName: Full=Adenylosuccinate synthetase; Short=AMPSase; Short=AdSS; EC=6.3.4.4; AltName: Full=IMP--aspartate ligase;. Gene name Name=purA Synonyms=adeK OrderedLocusNames=b4177, JW4135 Annotated species Escherichia coli [TaxID: 562] Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia. References [1]   MAPPING ON GEL PubMed=12469338; [NCBI, Expasy, EBI, Israel, Japan] Yan J.X., Devenish A.T., Wait R., Stone T., Lewis S., Fowler S. ''''''Fluorescence 2-D difference gel electrophoresis and mass spectrometry based proteomic analysis of E. coli'';'';'' Proteomics 2(1):1682-1698(2002) Comments SUBUNIT: HOMODIMER 2D PAGE maps for identified proteins How to interpret a protein ECOLI-DIGE4.5-6.5 {Escherichia coli DIGE (4.5-6.5)} Escherichia coli   map experimental info   protein estimated location   ECOLI-DIGE4.5-6.5 MAP LOCATIONS: SPOT 2D-001WKQ: pI=5.30; Mw=44524   [identification data] SPOT 2D-001WLA: pI=5.30; Mw=43494   [identification data] EXPRESSION: increase after benzoic acid treatment [1]. MAPPING (identification): SPOT 2D-001WKQ: Peptide mass fingerprinting [1]; SPOT 2D-001WLA: Tandem mass spectrometry [1]. Copyright This SWISS-2DPAGE entry is copyright the Swiss Institute of Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://world-2dpage.expasy.org/swiss-2dpage/docs/license.html or send email from legal@sib.swiss). Cross-references UniProtKB/Swiss-Prot P0A7D4; PURA_ECOLI. 2D PAGE maps for identified proteins How to interpret a protein map You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw. Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly. Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed. External data extracted from UniProtKB/Swiss-Prot Extracted from UniProtKB/Swiss-Prot, release: 2011_10 Entry name PURA_ECOLI Primary accession number P0A7D4 Secondary accession number(s) P12283 Q2M6C8 Sequence was last modified on  January 23, 2007 (version 2) Annotations were last modified on  October 19, 2011 (version 73) Name and origin of the protein Description RecName: Full=Adenylosuccinate synthetase; Short=AMPSase; Short=AdSS; EC=6.3.4.4; AltName: Full=IMP--aspartate ligase; Gene name Name=purA Synonyms=adeK OrderedLocusNames=b4177, JW4135 Encoded on Name=purA; Synonyms=adeK; OrderedLocusNames=b4177, JW4135 Keywords 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome. Copyright Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL J04199; AAA24446.1; -; Genomic_DNA EMBL U14003; AAA97073.1; -; Genomic_DNA EMBL U00096; AAC77134.1; -; Genomic_DNA EMBL AP009048; BAE78178.1; -; Genomic_DNA PIR S56402; AJECDS; . RefSeq NP_418598.1; NC_000913.2; . PDB 1ADE; X-ray; 2.00 A; A/B=2-432 PDB 1ADI; X-ray; 2.50 A; A/B=2-432 PDB 1CG0; X-ray; 2.50 A; A=2-432 PDB 1CG1; X-ray; 2.50 A; A=2-432 PDB 1CG3; X-ray; 2.50 A; A=2-432 PDB 1CG4; X-ray; 2.50 A; A=2-432 PDB 1CH8; X-ray; 2.50 A; A=2-432 PDB 1CIB; X-ray; 2.30 A; A=2-432 PDB 1GIM; X-ray; 2.50 A; A=2-432 PDB 1GIN; X-ray; 2.80 A; A=2-432 PDB 1HON; X-ray; 2.30 A; A/B=2-431 PDB 1HOO; X-ray; 2.30 A; A/B=2-431 PDB 1HOP; X-ray; 2.30 A; A/B=2-431 PDB 1JUY; X-ray; 2.50 A; A=2-432 PDB 1KJX; X-ray; 2.60 A; A=1-432 PDB 1KKB; X-ray; 2.60 A; A=1-432 PDB 1KKF; X-ray; 2.60 A; A=1-432 PDB 1KSZ; X-ray; 2.80 A; A=2-431 PDB 1NHT; X-ray; 2.50 A; A=2-431 PDB 1QF4; X-ray; 2.20 A; A=2-432 PDB 1QF5; X-ray; 2.00 A; A=2-432 PDB 1SON; X-ray; 2.55 A; A=2-431 PDB 1SOO; X-ray; 2.60 A; A=2-431 PDB 2GCQ; X-ray; 2.00 A; A=2-431 PDBsum 1ADE; -; . PDBsum 1ADI; -; . PDBsum 1CG0; -; . PDBsum 1CG1; -; . PDBsum 1CG3; -; . PDBsum 1CG4; -; . PDBsum 1CH8; -; . PDBsum 1CIB; -; . PDBsum 1GIM; -; . PDBsum 1GIN; -; . PDBsum 1HON; -; . PDBsum 1HOO; -; . PDBsum 1HOP; -; . PDBsum 1JUY; -; . PDBsum 1KJX; -; . PDBsum 1KKB; -; . PDBsum 1KKF; -; . PDBsum 1KSZ; -; . PDBsum 1NHT; -; . PDBsum 1QF4; -; . PDBsum 1QF5; -; . PDBsum 1SON; -; . PDBsum 1SOO; -; . PDBsum 2GCQ; -; . ProteinModelPortal P0A7D4; -; . SMR P0A7D4; 2-432; . DIP DIP-36219N; -; . IntAct P0A7D4; 2; . MINT MINT-1286548; -; . SWISS-2DPAGE P0A7D4; -; . PRIDE P0A7D4; -; . EnsemblBacteria EBESCT00000001008; EBESCP00000001008; EBESCG00000000829; . EnsemblBacteria EBESCT00000015695; EBESCP00000014986; EBESCG00000014755; . GeneID 948695; -; . GenomeReviews AP009048_GR; JW4135; . GenomeReviews U00096_GR; b4177; . KEGG ecj:JW4135; -; . KEGG eco:b4177; -; . EchoBASE EB0783; -; . EcoGene EG10790; purA; . eggNOG COG0104; -; . GeneTree EBGT00050000011605; -; . HOGENOM HBG658237; -; . OMA YVLGIIK; -; . ProtClustDB PRK01117; -; . BioCyc EcoCyc:ADENYLOSUCCINATE-SYN-MONOMER; -; . BioCyc MetaCyc:ADENYLOSUCCINATE-SYN-MONOMER; -; . DrugBank DB00131; Adenosine monophosphate; . Genevestigator P0A7D4; -; . GO GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell; . GO GO:0016020; C:membrane; IDA:UniProtKB; . GO GO:0004019; F:adenylosuccinate synthase activity; IDA:EcoCyc; . GO GO:0005525; F:GTP binding; IEA:UniProtKB-KW; . GO GO:0000287; F:magnesium ion binding; IEA:InterPro; . GO GO:0046086; P:adenosine biosynthetic process; IMP:EcoliWiki; . GO GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoliWiki; . GO GO:0006164; P:purine nucleotide biosynthetic process; IMP:EcoCyc; . HAMAP MF_00011; Adenylosucc_synth; 1; - InterPro IPR018220; Adenylosuccinate_synthase_AS; . InterPro IPR001114; Adenylosuccinate_synthetase; . PANTHER PTHR11846; Asucc_synthtase; 1; . Pfam PF00709; Adenylsucc_synt; 1; . SMART SM00788; Adenylsucc_synt; 1; . TIGRFAMs TIGR00184; PurA; 1; . PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1; . PROSITE PS00513; ADENYLOSUCCIN_SYN_2; 1; . SWISS-2DPAGE (search AC)