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SWISS-2DPAGE 
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Sample Preparation and Post-separation Analysis



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




SWISS-2DPAGE:  SUCD_ECOLI


SUCD_ECOLI


General information about the entry
View entry in simple text format
Entry nameSUCD_ECOLI
Primary accession numberP0AGE9
Secondary accession number(s) P07459
integrated into SWISS-2DPAGE on August 1, 1995 (release 2)
2D Annotations were last modified onMay 15, 2003 (version 3)
General Annotations were last modified on May 19, 2011 (version 12)
Name and origin of the protein
DescriptionRecName: Full=Succinyl-CoA ligase [ADP-forming] subunit alpha; EC=6.2.1.5; AltName: Full=Succinyl-CoA synthetase subunit alpha; Short=SCS-alpha;.
Gene nameName=sucD
OrderedLocusNames=b0729, JW0718
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
MEDLINE=80159887; PubMed=6988414; [NCBI, ExPASy, EBI, Israel, Japan]
Bloch P.L., Phillips T.A., Neidhardt F.C.
''''''Protein identifications of O'Farrell two-dimensional gels: locations of 81 Escherichia coli proteins'';'';''
J. Bacteriol. 141(1):1409-1420(1980)
[4]   MAPPING ON GEL
PubMed=11680886; [NCBI, ExPASy, EBI, Israel, Japan]
Tonella L., Hoogland C., Binz P.-A., Appel R.D., Hochstrasser D.F., Sanchez J.-C.
''''''New perspectives in the Escherichia coli proteome investigation'';'';''
Proteomics 1(1):409-423(2001)
Comments
  • SUBUNIT: TETRAMER OF TWO ALPHA AND TWO BETA CHAINS
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=6.16; Mw=31650

MAPPING (identification):
MICROSEQUENCE ANALYSIS [1] AND IDENTIFIED ON 2-D GELS BY VANBOGELEN [2] AND BLOCH [3].



ECOLI5.5-6.7 {Escherichia coli(5.5-6.7)}
Escherichia coli
ECOLI5.5-6.7
  map experimental info
  protein estimated location
 
ECOLI5.5-6.7

MAP LOCATIONS:
pI=5.86; Mw=28860

MAPPING (identification):
GEL MATCHING WITH ECOLI5-6 [4].



ECOLI5-6 {Escherichia coli(5-6)}
Escherichia coli
ECOLI5-6
  map experimental info
  protein estimated location
 
ECOLI5-6

MAP LOCATIONS:
pI=5.73; Mw=29525  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [4].

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
ECO2DBASEH028.0; 6TH EDITION.
UniProtKB/Swiss-ProtP0AGE9; SUCD_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 nameSUCD_ECOLI
Primary accession numberP0AGE9
Secondary accession number(s) P07459
Sequence was last modified on January 23, 2007 (version 2)
Annotations were last modified on October 19, 2011 (version 57)
Name and origin of the protein
DescriptionRecName: Full=Succinyl-CoA ligase [ADP-forming] subunit alpha; EC=6.2.1.5; AltName: Full=Succinyl-CoA synthetase subunit alpha; Short=SCS-alpha;
Gene nameName=sucD
OrderedLocusNames=b0729, JW0718
Encoded onName=sucD; OrderedLocusNames=b0729, JW0718
Keywords3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; Reference proteome; Tricarboxylic acid cycle.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLJ01619; AAA23900.1; -; Genomic_DNA
EMBLU00096; AAC73823.1; -; Genomic_DNA
EMBLAP009048; BAA35395.1; -; Genomic_DNA
EMBLX15790; CAA33792.1; -; Genomic_DNA
PIRA90499; SYECSA; .
RefSeqNP_415257.1; NC_000913.2; .
PDB1CQI; X-ray; 3.30 A; A/D=2-287
PDB1CQJ; X-ray; 2.90 A; A/D=2-287
PDB1JKJ; X-ray; 2.35 A; A/D=1-289
PDB1JLL; X-ray; 2.69 A; A/D=1-289
PDB1SCU; X-ray; 2.50 A; A/D=2-289
PDB2NU6; X-ray; 2.55 A; A/D=2-288
PDB2NU7; X-ray; 2.20 A; A/D=2-288
PDB2NU8; X-ray; 2.15 A; A/D=2-288
PDB2NU9; X-ray; 2.90 A; A/D/F/H=2-289
PDB2NUA; X-ray; 2.95 A; A/D=2-288
PDB2SCU; X-ray; 2.30 A; A/D=2-289
PDBsum1CQI; -; .
PDBsum1CQJ; -; .
PDBsum1JKJ; -; .
PDBsum1JLL; -; .
PDBsum1SCU; -; .
PDBsum2NU6; -; .
PDBsum2NU7; -; .
PDBsum2NU8; -; .
PDBsum2NU9; -; .
PDBsum2NUA; -; .
PDBsum2SCU; -; .
ProteinModelPortalP0AGE9; -; .
SMRP0AGE9; 2-288; .
DIPDIP-31851N; -; .
IntActP0AGE9; 7; .
MINTMINT-1219451; -; .
SWISS-2DPAGEP0AGE9; -; .
ECO2DBASEH028.0; 6TH EDITION; .
PRIDEP0AGE9; -; .
EnsemblBacteriaEBESCT00000004064; EBESCP00000004064; EBESCG00000003319; .
EnsemblBacteriaEBESCT00000004065; EBESCP00000004065; EBESCG00000003319; .
EnsemblBacteriaEBESCT00000014676; EBESCP00000013967; EBESCG00000013737; .
GeneID945314; -; .
GenomeReviewsAP009048_GR; JW0718; .
GenomeReviewsU00096_GR; b0729; .
KEGGecj:JW0718; -; .
KEGGeco:b0729; -; .
EchoBASEEB0975; -; .
EcoGeneEG10982; sucD; .
eggNOGCOG0074; -; .
GeneTreeEBGT00050000010106; -; .
HOGENOMHBG615372; -; .
OMADETTEAI; -; .
ProtClustDBPRK05678; -; .
BioCycEcoCyc:SUCCCOASYN-ALPHA; -; .
BioCycMetaCyc:SUCCCOASYN-ALPHA; -; .
GenevestigatorP0AGE9; -; .
GOGO:0005737; C:cytoplasm; IDA:UniProtKB; .
GOGO:0005524; F:ATP binding; IEA:UniProtKB-KW; .
GOGO:0003878; F:ATP citrate synthase activity; IEA:InterPro; .
GOGO:0005515; F:protein binding; IPI:IntAct; .
GOGO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:EC; .
GOGO:0006099; P:tricarboxylic acid cycle; IDA:EcoliWiki; .
InterProIPR017440; Cit_synth/succinyl-CoA_lig_AS; .
InterProIPR003781; CoA-bd; .
InterProIPR005810; CoA_lig_alpha; .
InterProIPR005811; CoA_ligase; .
InterProIPR016040; NAD(P)-bd_dom; .
InterProIPR016102; Succinyl-CoA_synth-like; .
Gene3DG3DSA:3.40.50.720; NAD(P)-bd; 1; .
Gene3DG3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1; .
PfamPF02629; CoA_binding; 1; .
PfamPF00549; Ligase_CoA; 1; .
PIRSFPIRSF001553; SucCS_alpha; 1; .
PRINTSPR01798; SCOASYNTHASE; .
SMARTSM00881; CoA_binding; 1; .
SUPFAMSSF52210; CoA_ligase; 1; .
TIGRFAMsTIGR01019; SucCoAalpha; 1; .
PROSITEPS01216; SUCCINYL_COA_LIG_1; 1; .
PROSITEPS00399; SUCCINYL_COA_LIG_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