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Sample Preparation and Post-separation Analysis Searching in 'SWISS-2DPAGE' for entry matching: DYR_ECOLI SWISS-2DPAGE:  DYR_ECOLI DYR_ECOLI General information about the entry View entry in simple text format Entry name DYR_ECOLI Primary accession number P0ABQ4 Secondary accession number(s) P00379 integrated into SWISS-2DPAGE on  August 1, 1995 (release 2) 2D Annotations were last modified on March 31, 2004 (version 2) General Annotations were last modified on  May 19, 2011 (version 12) Name and origin of the protein Description RecName: Full=Dihydrofolate reductase; EC=1.5.1.3;. Gene name Name=folA Synonyms=tmrA OrderedLocusNames=b0048, JW0047 Annotated species Escherichia coli [TaxID: 562] Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia. References [1]   MAPPING ON GEL MEDLINE=96314059; PubMed=8740179; [NCBI, Expasy, EBI, Israel, Japan] Pasquali C., Frutiger S., Wilkins M.R., Hughes G.J., Appel R.D., Bairoch A., Schaller D., Sanchez J.-C., Hochstrasser D.F. ''''''Two-dimensional gel electrophoresis of Escherichia coli homogenates: the Escherichia coli SWISS-2DPAGE database'';'';'' Electrophoresis 17(1):547-555(1996) [2]   MAPPING ON GEL Vanbogelen R.A., Abshire K.Z., Pertsemlidis A., Clark R.L., Neidhardt F.C. ''''''Gene-protein database of Escherichia coli K-12, edition 6'';'';'' (IN) Neidhardt et al. (eds.)Escherichia coli and Salmonella: Cellular and Molecular Biology (2nd ed.), pp.2067-2117, ASM Press, Washington DC (1996) [3]   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) 2D PAGE maps for identified proteins How to interpret a protein ECOLI {Escherichia coli} Escherichia coli   map experimental info   protein estimated location   ECOLI MAP LOCATIONS: SPOT 2D-000LM1: pI=5.01; Mw=19992 MAPPING (identification): GEL MATCHING [1] AND IDENTIFIED ON 2-D GELS BY VANBOGELEN [2]. 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-001WVR: pI=5.02; Mw=21096   [identification data] EXPRESSION: decrease after benzoic acid treatment [3]. MAPPING (identification): Tandem mass spectrometry [3]. 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 ECO2DBASE B020.0; 6TH EDITION. UniProtKB/Swiss-Prot P0ABQ4; DYR_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 DYR_ECOLI Primary accession number P0ABQ4 Secondary accession number(s) P00379 Sequence was last modified on  July 21, 1986 (version 1) Annotations were last modified on  October 19, 2011 (version 67) Name and origin of the protein Description RecName: Full=Dihydrofolate reductase; EC=1.5.1.3; Gene name Name=folA Synonyms=tmrA OrderedLocusNames=b0048, JW0047 Encoded on Name=folA; Synonyms=tmrA; OrderedLocusNames=b0048, JW0047 Keywords 3D-structure; Antibiotic resistance; Complete proteome; Direct protein sequencing; Methotrexate resistance; NADP; One-carbon metabolism; Oxidoreductase; Reference proteome; Trimethoprim resistance. Copyright Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL J01609; AAA87976.1; -; Genomic_DNA EMBL X05108; CAA28755.1; -; Genomic_DNA EMBL U00096; AAC73159.1; -; Genomic_DNA EMBL AP009048; BAB96616.1; -; Genomic_DNA PIR A93704; RDECD; . RefSeq NP_414590.1; NC_000913.2; . PDB 1DDR; X-ray; 2.45 A; A/B=1-159 PDB 1DDS; X-ray; 2.20 A; A/B=1-159 PDB 1DHI; X-ray; 1.90 A; A/B=1-159 PDB 1DHJ; X-ray; 1.80 A; A/B=1-159 PDB 1DRA; X-ray; 1.90 A; A/B=1-159 PDB 1DRB; X-ray; 1.96 A; A/B=1-159 PDB 1DRE; X-ray; 2.60 A; A=1-159 PDB 1DRH; X-ray; 2.30 A; A=1-159 PDB 1DYH; X-ray; 1.90 A; A/B=1-159 PDB 1DYI; X-ray; 1.90 A; A/B=1-159 PDB 1DYJ; X-ray; 1.85 A; A/B=1-159 PDB 1JOL; X-ray; 1.96 A; A/B=1-159 PDB 1JOM; X-ray; 1.90 A; A=1-159 PDB 1RA1; X-ray; 1.90 A; A=1-159 PDB 1RA2; X-ray; 1.60 A; A=1-159 PDB 1RA3; X-ray; 1.80 A; A=1-159 PDB 1RA8; X-ray; 1.80 A; A=1-159 PDB 1RA9; X-ray; 1.55 A; A=1-159 PDB 1RB2; X-ray; 2.10 A; A/B=1-159 PDB 1RB3; X-ray; 2.30 A; A/B=1-159 PDB 1RC4; X-ray; 1.90 A; A=1-159 PDB 1RD7; X-ray; 2.60 A; A/B=1-159 PDB 1RE7; X-ray; 2.60 A; A/B=1-159 PDB 1RF7; X-ray; 1.80 A; A=1-159 PDB 1RG7; X-ray; 2.00 A; A=1-159 PDB 1RH3; X-ray; 2.40 A; A=1-159 PDB 1RX1; X-ray; 2.00 A; A=1-159 PDB 1RX2; X-ray; 1.80 A; A=1-159 PDB 1RX3; X-ray; 2.20 A; A=1-159 PDB 1RX4; X-ray; 2.20 A; A=1-159 PDB 1RX5; X-ray; 2.30 A; A=1-159 PDB 1RX6; X-ray; 2.00 A; A=1-159 PDB 1RX7; X-ray; 2.30 A; A=1-159 PDB 1RX8; X-ray; 2.80 A; A=1-159 PDB 1RX9; X-ray; 1.90 A; A=1-159 PDB 1TDR; X-ray; 2.50 A; A/B=1-159 PDB 2ANO; X-ray; 2.68 A; A=1-159 PDB 2ANQ; X-ray; 2.13 A; A=1-159 PDB 2D0K; X-ray; 1.90 A; A/B=2-159 PDB 2DRC; X-ray; 1.90 A; A/B=1-159 PDB 2INQ; Neutron; 2.20 A; A/B=1-159 PDB 3DAU; X-ray; 1.50 A; A=1-159 PDB 3DRC; X-ray; 1.90 A; A/B=1-159 PDB 3K74; X-ray; 1.95 A; A=1-159 PDB 3KFY; X-ray; 2.08 A; A=1-159 PDB 3OCH; X-ray; 1.79 A; A/B=1-159 PDB 3QL3; X-ray; 1.80 A; A=1-159 PDB 4DFR; X-ray; 1.70 A; A/B=1-159 PDB 5DFR; X-ray; 2.30 A; A=1-159 PDB 6DFR; X-ray; 2.40 A; A=1-159 PDB 7DFR; X-ray; 2.50 A; A=1-159 PDBsum 1DDR; -; . PDBsum 1DDS; -; . PDBsum 1DHI; -; . PDBsum 1DHJ; -; . PDBsum 1DRA; -; . PDBsum 1DRB; -; . PDBsum 1DRE; -; . PDBsum 1DRH; -; . PDBsum 1DYH; -; . PDBsum 1DYI; -; . PDBsum 1DYJ; -; . PDBsum 1JOL; -; . PDBsum 1JOM; -; . PDBsum 1RA1; -; . PDBsum 1RA2; -; . PDBsum 1RA3; -; . PDBsum 1RA8; -; . PDBsum 1RA9; -; . PDBsum 1RB2; -; . PDBsum 1RB3; -; . PDBsum 1RC4; -; . PDBsum 1RD7; -; . PDBsum 1RE7; -; . PDBsum 1RF7; -; . PDBsum 1RG7; -; . PDBsum 1RH3; -; . PDBsum 1RX1; -; . PDBsum 1RX2; -; . PDBsum 1RX3; -; . PDBsum 1RX4; -; . PDBsum 1RX5; -; . PDBsum 1RX6; -; . PDBsum 1RX7; -; . PDBsum 1RX8; -; . PDBsum 1RX9; -; . PDBsum 1TDR; -; . PDBsum 2ANO; -; . PDBsum 2ANQ; -; . PDBsum 2D0K; -; . PDBsum 2DRC; -; . PDBsum 2INQ; -; . PDBsum 3DAU; -; . PDBsum 3DRC; -; . PDBsum 3K74; -; . PDBsum 3KFY; -; . PDBsum 3OCH; -; . PDBsum 3QL3; -; . PDBsum 4DFR; -; . PDBsum 5DFR; -; . PDBsum 6DFR; -; . PDBsum 7DFR; -; . ProteinModelPortal P0ABQ4; -; . SMR P0ABQ4; 1-159; . DIP DIP-35824N; -; . IntAct P0ABQ4; 10; . MINT MINT-1239602; -; . SWISS-2DPAGE P0ABQ4; -; . ECO2DBASE B020.0; 6TH EDITION; . EnsemblBacteria EBESCT00000002161; EBESCP00000002161; EBESCG00000001770; . EnsemblBacteria EBESCT00000015691; EBESCP00000014982; EBESCG00000014751; . GeneID 944790; -; . GenomeReviews AP009048_GR; JW0047; . GenomeReviews U00096_GR; b0048; . KEGG ecj:JW0047; -; . KEGG eco:b0048; -; . EchoBASE EB0322; -; . EcoGene EG10326; folA; . eggNOG COG0262; -; . GeneTree EBGT00050000010807; -; . HOGENOM HBG665708; -; . OMA PTRFVVY; -; . ProtClustDB PRK10769; -; . BioCyc EcoCyc:DIHYDROFOLATEREDUCT-MONOMER; -; . BioCyc MetaCyc:DIHYDROFOLATEREDUCT-MONOMER; -; . BindingDB P0ABQ4; -; . Genevestigator P0ABQ4; -; . GO GO:0004146; F:dihydrofolate reductase activity; IEA:EC; . GO GO:0004151; F:dihydroorotase activity; IDA:EcoCyc; . GO GO:0050661; F:NADP binding; IEA:InterPro; . GO GO:0008270; F:zinc ion binding; IDA:EcoCyc; . GO GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IMP:EcoCyc; . GO GO:0006545; P:glycine biosynthetic process; IEA:InterPro; . GO GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro; . GO GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW; . GO GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW; . GO GO:0031427; P:response to methotrexate; IEA:UniProtKB-KW; . InterPro IPR012259; DHFR; . InterPro IPR024072; DHFR-like_dom; . InterPro IPR017925; DHFR_CS; . InterPro IPR001796; DHFR_dom; . Gene3D G3DSA:3.40.430.10; G3DSA:3.40.430.10; 1; . Pfam PF00186; DHFR_1; 1; . PRINTS PR00070; DHFR; . SUPFAM SSF53597; SSF53597; 1; . PROSITE PS00075; DHFR_1; 1; . PROSITE PS51330; DHFR_2; 1; . SWISS-2DPAGE (search AC)