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SWISS-2DPAGE 
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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: P0A9P0




SWISS-2DPAGE:  P0A9P0


P0A9P0


General information about the entry
View entry in simple text format
Entry nameDLDH_ECOLI
Primary accession numberP0A9P0
Secondary accession number(s) P00391
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 14)
Name and origin of the protein
DescriptionRecName: Full=Dihydrolipoyl dehydrogenase; EC=1.8.1.4; AltName: Full=Dihydrolipoamide dehydrogenase; AltName: Full=E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; AltName: Full=Glycine cleavage system L protein;.
Gene nameName=lpdA
Synonyms=lpd
OrderedLocusNames=b0116, JW0112
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]   PROTEIN EXPRESSION
MEDLINE=87194592; PubMed=3553157; [NCBI, ExPASy, EBI, Israel, Japan]
Jones P.G., Vanbogelen R.A., Neidhardt F.C.
''''''Induction of proteins in response to low temperature in Escherichia coli'';'';''
J. Bacteriol. 169(1):2092-2095(1987)
[4]   PROTEIN EXPRESSION
MEDLINE=83160794; PubMed=6339477; [NCBI, ExPASy, EBI, Israel, Japan]
Smith M.W., Neidhardt F.C.
''''''Proteins induced by aerobiosis in Escherichia coli'';'';''
J. Bacteriol. 154(1):344-350(1983)
[5]   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 {Escherichia coli}
Escherichia coli
ECOLI
  map experimental info
  protein estimated location
 
ECOLI

MAP LOCATIONS:
pI=5.81; Mw=53704

EXPRESSION:
INCREASED DURING AEROBIC GROWTH [4]; INCREASED DURING THE ADJUSTMENT OF E. COLI TO GROWTH AT 10C [3].

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=5.82; Mw=50800  [identification data]
pI=5.90; Mw=28059  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [5];
SPOT 2D-001WS6: TANDEM MASS SPECTROMETRY [5].

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
2DBase-EcoliP0A9P0; DLDH_ECOLI.
ECO2DBASEG050.5; 6TH EDITION.
UniProtKB/Swiss-ProtP0A9P0; DLDH_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 nameDLDH_ECOLI
Primary accession numberP0A9P0
Secondary accession number(s) P00391
Sequence was last modified on January 23, 2007 (version 2)
Annotations were last modified on October 19, 2011 (version 64)
Name and origin of the protein
DescriptionRecName: Full=Dihydrolipoyl dehydrogenase; EC=1.8.1.4; AltName: Full=Dihydrolipoamide dehydrogenase; AltName: Full=E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; AltName: Full=Glycine cleavage system L protein;
Gene nameName=lpdA
Synonyms=lpd
OrderedLocusNames=b0116, JW0112
Encoded onName=lpdA; Synonyms=lpd; OrderedLocusNames=b0116, JW0112
KeywordsAcetylation; Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycolysis; Membrane; NAD; Oxidoreductase; Redox-active center; 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
EMBLV01498; CAA24742.1; ALT_INIT; Genomic_DNA
EMBLU00096; AAC73227.1; -; Genomic_DNA
EMBLAP009048; BAB96686.2; -; Genomic_DNA
PIRS45195; DEECLP; .
RefSeqNP_414658.1; NC_000913.2; .
ProteinModelPortalP0A9P0; -; .
SMRP0A9P0; 19-470; .
IntActP0A9P0; 90; .
MINTMINT-1242510; -; .
SWISS-2DPAGEP0A9P0; -; .
2DBase-EcoliP0A9P0; -; .
ECO2DBASEG050.5; 6TH EDITION; .
EnsemblBacteriaEBESCT00000002234; EBESCP00000002234; EBESCG00000001831; .
EnsemblBacteriaEBESCT00000002235; EBESCP00000002235; EBESCG00000001831; .
EnsemblBacteriaEBESCT00000016832; EBESCP00000016123; EBESCG00000015891; .
GeneID944854; -; .
GenomeReviewsAP009048_GR; JW0112; .
GenomeReviewsU00096_GR; b0116; .
KEGGecj:JW0112; -; .
KEGGeco:b0116; -; .
EchoBASEEB0538; -; .
EcoGeneEG10543; lpd; .
eggNOGCOG1249; -; .
GeneTreeEBGT00050000009315; -; .
HOGENOMHBG515043; -; .
OMAMMDGLMA; -; .
ProtClustDBPRK06467; -; .
BioCycEcoCyc:E3-MONOMER; -; .
BioCycMetaCyc:E3-MONOMER; -; .
GenevestigatorP0A9P0; -; .
GOGO:0005829; C:cytosol; IDA:UniProtKB; .
GOGO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell; .
GOGO:0004148; F:dihydrolipoyl dehydrogenase activity; IDA:EcoliWiki; .
GOGO:0015036; F:disulfide oxidoreductase activity; IDA:EcoliWiki; .
GOGO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoliWiki; .
GOGO:0005515; F:protein binding; IPI:IntAct; .
GOGO:0008270; F:zinc ion binding; IDA:EcoliWiki; .
GOGO:0006103; P:2-oxoglutarate metabolic process; IMP:EcoliWiki; .
GOGO:0045454; P:cell redox homeostasis; IEA:InterPro; .
GOGO:0019464; P:glycine decarboxylation via glycine cleavage system; IMP:EcoCyc; .
GOGO:0006096; P:glycolysis; IEA:UniProtKB-KW; .
GOGO:0006090; P:pyruvate metabolic process; IDA:EcoliWiki; .
GOGO:0006099; P:tricarboxylic acid cycle; IDA:EcoliWiki; .
InterProIPR016156; FAD/NAD-linked_Rdtase_dimer; .
InterProIPR013027; FAD_pyr_nucl-diS_OxRdtase; .
InterProIPR006258; Lipoamide_DH; .
InterProIPR004099; Pyr_nucl-diS_OxRdtase_dimer; .
InterProIPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD; .
InterProIPR012999; Pyr_OxRdtase_I_AS; .
InterProIPR001327; Pyr_OxRdtase_NAD-bd_dom; .
Gene3DG3DSA:3.30.390.30; Pyr_redox_dim; 1; .
PANTHERPTHR22912:SF20; Lipoamide_DH; 1; .
PfamPF00070; Pyr_redox; 1; .
PfamPF07992; Pyr_redox_2; 1; .
PfamPF02852; Pyr_redox_dim; 1; .
PRINTSPR00368; FADPNR; .
SUPFAMSSF55424; FAD/NAD-linked_reductase_dimer; 1; .
TIGRFAMsTIGR01350; Lipoamide_DH; 1; .
PROSITEPS00076; PYRIDINE_REDOX_1; 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