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SWISS-2DPAGE 
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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 nameDYR_ECOLI
Primary accession numberP0ABQ4
Secondary accession number(s) P00379
integrated into SWISS-2DPAGE on August 1, 1995 (release 2)
2D Annotations were last modified onMarch 31, 2004 (version 2)
General Annotations were last modified on May 19, 2011 (version 12)
Name and origin of the protein
DescriptionRecName: Full=Dihydrofolate reductase; EC=1.5.1.3;.
Gene nameName=folA
Synonyms=tmrA
OrderedLocusNames=b0048, JW0047
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; 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
ECOLI
  map experimental info
  protein estimated location
 
ECOLI

MAP LOCATIONS:
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
ECOLI-DIGE4.5-6.5
  map experimental info
  protein estimated location
 
ECOLI-DIGE4.5-6.5

MAP LOCATIONS:
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
ECO2DBASEB020.0; 6TH EDITION.
UniProtKB/Swiss-ProtP0ABQ4; 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 nameDYR_ECOLI
Primary accession numberP0ABQ4
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
DescriptionRecName: Full=Dihydrofolate reductase; EC=1.5.1.3;
Gene nameName=folA
Synonyms=tmrA
OrderedLocusNames=b0048, JW0047
Encoded onName=folA; Synonyms=tmrA; OrderedLocusNames=b0048, JW0047
Keywords3D-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
EMBLJ01609; AAA87976.1; -; Genomic_DNA
EMBLX05108; CAA28755.1; -; Genomic_DNA
EMBLU00096; AAC73159.1; -; Genomic_DNA
EMBLAP009048; BAB96616.1; -; Genomic_DNA
PIRA93704; RDECD; .
RefSeqNP_414590.1; NC_000913.2; .
PDB1DDR; X-ray; 2.45 A; A/B=1-159
PDB1DDS; X-ray; 2.20 A; A/B=1-159
PDB1DHI; X-ray; 1.90 A; A/B=1-159
PDB1DHJ; X-ray; 1.80 A; A/B=1-159
PDB1DRA; X-ray; 1.90 A; A/B=1-159
PDB1DRB; X-ray; 1.96 A; A/B=1-159
PDB1DRE; X-ray; 2.60 A; A=1-159
PDB1DRH; X-ray; 2.30 A; A=1-159
PDB1DYH; X-ray; 1.90 A; A/B=1-159
PDB1DYI; X-ray; 1.90 A; A/B=1-159
PDB1DYJ; X-ray; 1.85 A; A/B=1-159
PDB1JOL; X-ray; 1.96 A; A/B=1-159
PDB1JOM; X-ray; 1.90 A; A=1-159
PDB1RA1; X-ray; 1.90 A; A=1-159
PDB1RA2; X-ray; 1.60 A; A=1-159
PDB1RA3; X-ray; 1.80 A; A=1-159
PDB1RA8; X-ray; 1.80 A; A=1-159
PDB1RA9; X-ray; 1.55 A; A=1-159
PDB1RB2; X-ray; 2.10 A; A/B=1-159
PDB1RB3; X-ray; 2.30 A; A/B=1-159
PDB1RC4; X-ray; 1.90 A; A=1-159
PDB1RD7; X-ray; 2.60 A; A/B=1-159
PDB1RE7; X-ray; 2.60 A; A/B=1-159
PDB1RF7; X-ray; 1.80 A; A=1-159
PDB1RG7; X-ray; 2.00 A; A=1-159
PDB1RH3; X-ray; 2.40 A; A=1-159
PDB1RX1; X-ray; 2.00 A; A=1-159
PDB1RX2; X-ray; 1.80 A; A=1-159
PDB1RX3; X-ray; 2.20 A; A=1-159
PDB1RX4; X-ray; 2.20 A; A=1-159
PDB1RX5; X-ray; 2.30 A; A=1-159
PDB1RX6; X-ray; 2.00 A; A=1-159
PDB1RX7; X-ray; 2.30 A; A=1-159
PDB1RX8; X-ray; 2.80 A; A=1-159
PDB1RX9; X-ray; 1.90 A; A=1-159
PDB1TDR; X-ray; 2.50 A; A/B=1-159
PDB2ANO; X-ray; 2.68 A; A=1-159
PDB2ANQ; X-ray; 2.13 A; A=1-159
PDB2D0K; X-ray; 1.90 A; A/B=2-159
PDB2DRC; X-ray; 1.90 A; A/B=1-159
PDB2INQ; Neutron; 2.20 A; A/B=1-159
PDB3DAU; X-ray; 1.50 A; A=1-159
PDB3DRC; X-ray; 1.90 A; A/B=1-159
PDB3K74; X-ray; 1.95 A; A=1-159
PDB3KFY; X-ray; 2.08 A; A=1-159
PDB3OCH; X-ray; 1.79 A; A/B=1-159
PDB3QL3; X-ray; 1.80 A; A=1-159
PDB4DFR; X-ray; 1.70 A; A/B=1-159
PDB5DFR; X-ray; 2.30 A; A=1-159
PDB6DFR; X-ray; 2.40 A; A=1-159
PDB7DFR; X-ray; 2.50 A; A=1-159
PDBsum1DDR; -; .
PDBsum1DDS; -; .
PDBsum1DHI; -; .
PDBsum1DHJ; -; .
PDBsum1DRA; -; .
PDBsum1DRB; -; .
PDBsum1DRE; -; .
PDBsum1DRH; -; .
PDBsum1DYH; -; .
PDBsum1DYI; -; .
PDBsum1DYJ; -; .
PDBsum1JOL; -; .
PDBsum1JOM; -; .
PDBsum1RA1; -; .
PDBsum1RA2; -; .
PDBsum1RA3; -; .
PDBsum1RA8; -; .
PDBsum1RA9; -; .
PDBsum1RB2; -; .
PDBsum1RB3; -; .
PDBsum1RC4; -; .
PDBsum1RD7; -; .
PDBsum1RE7; -; .
PDBsum1RF7; -; .
PDBsum1RG7; -; .
PDBsum1RH3; -; .
PDBsum1RX1; -; .
PDBsum1RX2; -; .
PDBsum1RX3; -; .
PDBsum1RX4; -; .
PDBsum1RX5; -; .
PDBsum1RX6; -; .
PDBsum1RX7; -; .
PDBsum1RX8; -; .
PDBsum1RX9; -; .
PDBsum1TDR; -; .
PDBsum2ANO; -; .
PDBsum2ANQ; -; .
PDBsum2D0K; -; .
PDBsum2DRC; -; .
PDBsum2INQ; -; .
PDBsum3DAU; -; .
PDBsum3DRC; -; .
PDBsum3K74; -; .
PDBsum3KFY; -; .
PDBsum3OCH; -; .
PDBsum3QL3; -; .
PDBsum4DFR; -; .
PDBsum5DFR; -; .
PDBsum6DFR; -; .
PDBsum7DFR; -; .
ProteinModelPortalP0ABQ4; -; .
SMRP0ABQ4; 1-159; .
DIPDIP-35824N; -; .
IntActP0ABQ4; 10; .
MINTMINT-1239602; -; .
SWISS-2DPAGEP0ABQ4; -; .
ECO2DBASEB020.0; 6TH EDITION; .
EnsemblBacteriaEBESCT00000002161; EBESCP00000002161; EBESCG00000001770; .
EnsemblBacteriaEBESCT00000015691; EBESCP00000014982; EBESCG00000014751; .
GeneID944790; -; .
GenomeReviewsAP009048_GR; JW0047; .
GenomeReviewsU00096_GR; b0048; .
KEGGecj:JW0047; -; .
KEGGeco:b0048; -; .
EchoBASEEB0322; -; .
EcoGeneEG10326; folA; .
eggNOGCOG0262; -; .
GeneTreeEBGT00050000010807; -; .
HOGENOMHBG665708; -; .
OMAPTRFVVY; -; .
ProtClustDBPRK10769; -; .
BioCycEcoCyc:DIHYDROFOLATEREDUCT-MONOMER; -; .
BioCycMetaCyc:DIHYDROFOLATEREDUCT-MONOMER; -; .
BindingDBP0ABQ4; -; .
GenevestigatorP0ABQ4; -; .
GOGO:0004146; F:dihydrofolate reductase activity; IEA:EC; .
GOGO:0004151; F:dihydroorotase activity; IDA:EcoCyc; .
GOGO:0050661; F:NADP binding; IEA:InterPro; .
GOGO:0008270; F:zinc ion binding; IDA:EcoCyc; .
GOGO:0006207; P:'de novo' pyrimidine base biosynthetic process; IMP:EcoCyc; .
GOGO:0006545; P:glycine biosynthetic process; IEA:InterPro; .
GOGO:0009165; P:nucleotide biosynthetic process; IEA:InterPro; .
GOGO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW; .
GOGO:0046677; P:response to antibiotic; IEA:UniProtKB-KW; .
GOGO:0031427; P:response to methotrexate; IEA:UniProtKB-KW; .
InterProIPR012259; DHFR; .
InterProIPR024072; DHFR-like_dom; .
InterProIPR017925; DHFR_CS; .
InterProIPR001796; DHFR_dom; .
Gene3DG3DSA:3.40.430.10; G3DSA:3.40.430.10; 1; .
PfamPF00186; DHFR_1; 1; .
PRINTSPR00070; DHFR; .
SUPFAMSSF53597; SSF53597; 1; .
PROSITEPS00075; DHFR_1; 1; .
PROSITEPS51330; DHFR_2; 1; .



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Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server