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SWISS-2DPAGE 
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Searching in 'SWISS-2DPAGE' for entry matching: P36683




SWISS-2DPAGE:  P36683


P36683


General information about the entry
View entry in simple text format
Entry nameACON2_ECOLI
Primary accession numberP36683
integrated into SWISS-2DPAGE on October 1, 1998 (release 8)
2D Annotations were last modified onMay 15, 2003 (version 2)
General Annotations were last modified on May 19, 2011 (version 13)
Name and origin of the protein
DescriptionRecName: Full=Aconitate hydratase 2; Short=Aconitase; EC=4.2.1.3; AltName: Full=2-methylisocitrate dehydratase; EC=4.2.1.99; AltName: Full=Citrate hydro-lyase;.
Gene nameName=acnB
Synonyms=yacI, yacJ
OrderedLocusNames=b0118, JW0114
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   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)
[2]   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

ECOLI4.5-5.5 {Escherichia coli(4.5-5.5)}
Escherichia coli
ECOLI4.5-5.5
  map experimental info
  protein estimated location
 
ECOLI4.5-5.5

MAP LOCATIONS:
pI=5.24; Mw=92389  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [1].



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=5.30; Mw=95000  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [2].

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-ProtP36683; ACON2_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 nameACON2_ECOLI
Primary accession numberP36683
Secondary accession number(s) P36648 P75652 Q59382
Sequence was last modified on November 1, 1997 (version 3)
Annotations were last modified on October 19, 2011 (version 112)
Name and origin of the protein
DescriptionRecName: Full=Aconitate hydratase 2; Short=Aconitase; EC=4.2.1.3; AltName: Full=2-methylisocitrate dehydratase; EC=4.2.1.99; AltName: Full=Citrate hydro-lyase;
Gene nameName=acnB
Synonyms=yacI, yacJ
OrderedLocusNames=b0118, JW0114
Encoded onName=acnB; Synonyms=yacI, yacJ; OrderedLocusNames=b0118, JW0114
Keywords3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding; 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
EMBLU00096; AAC73229.1; -; Genomic_DNA
EMBLAP009048; BAB96692.2; -; Genomic_DNA
EMBLU41560; AAC43710.1; -; Genomic_DNA
PIRF64734; F64734; .
RefSeqNP_414660.1; NC_000913.2; .
PDB1L5J; X-ray; 2.40 A; A/B=1-865
PDBsum1L5J; -; .
ProteinModelPortalP36683; -; .
SMRP36683; 1-862; .
DIPDIP-9044N; -; .
IntActP36683; 15; .
PhosSiteP36683; -; .
SWISS-2DPAGEP36683; -; .
PRIDEP36683; -; .
EnsemblBacteriaEBESCT00000000659; EBESCP00000000659; EBESCG00000000550; .
EnsemblBacteriaEBESCT00000014483; EBESCP00000013774; EBESCG00000013544; .
GeneID944864; -; .
GenomeReviewsAP009048_GR; JW0114; .
GenomeReviewsU00096_GR; b0118; .
KEGGecj:JW0114; -; .
KEGGeco:b0118; -; .
EchoBASEEB2222; -; .
EcoGeneEG12316; acnB; .
eggNOGCOG1049; -; .
GeneTreeEBGT00050000008227; -; .
HOGENOMHBG284496; -; .
OMAGVRPGMY; -; .
ProtClustDBPRK09238; -; .
BioCycEcoCyc:ACONITATEDEHYDRB-MONOMER; -; .
BioCycMetaCyc:ACONITATEDEHYDRB-MONOMER; -; .
BRENDA4.2.1.3; 2026; .
GenevestigatorP36683; -; .
GOGO:0047456; F:2-methylisocitrate dehydratase activity; IDA:EcoCyc; .
GOGO:0051539; F:4 iron; 4 sulfur cluster binding; IDA:EcoCyc
GOGO:0003994; F:aconitate hydratase activity; IDA:EcoCyc; .
GOGO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC; .
GOGO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC; .
GOGO:0046872; F:metal ion binding; IEA:UniProtKB-KW; .
GOGO:0003730; F:mRNA 3'-UTR binding; IDA:EcoCyc; .
GOGO:0019629; P:propionate catabolic process; 2-methylcitrate cycle; IDA:EcoCyc
GOGO:0006417; P:regulation of translation; IDA:EcoCyc; .
GOGO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW; .
InterProIPR015931; Acnase/IPM_dHydase_lsu_aba_1/3; .
InterProIPR015937; Acoase/IPM_deHydtase; .
InterProIPR001030; Acoase/IPM_deHydtase_lsu_aba; .
InterProIPR015928; Aconitase/3IPM_dehydase_swvl; .
InterProIPR018136; Aconitase_4Fe-4S_BS; .
InterProIPR004406; Aconitase_B_bac; .
InterProIPR015930; Aconitase_B_FeS-bd_bac; .
InterProIPR015933; Aconitase_B_HEAT-like_bac; .
InterProIPR015929; Aconitase_B_N_bac; .
Gene3DG3DSA:3.30.499.10; Acnase/IPM_dHydase_lsu_aba_1/3; 2; .
Gene3DG3DSA:3.20.19.10; Aconitase/3IPM_dehydase_swvl; 1; .
PANTHERPTHR11670; Aconitase-like_core; 1; .
PANTHERPTHR11670:SF3; Aconitase_2; 1; .
PfamPF00330; Aconitase; 2; .
PfamPF06434; Aconitase_2_N; 1; .
PfamPF11791; Aconitase_B_N; 1; .
PIRSFPIRSF036687; AcnB; 1; .
SUPFAMSSF52016; Aconitase/3IPM_dehydase_swvl; 1; .
SUPFAMSSF74778; Aconitase_B_HEAT-like_bac; 1; .
SUPFAMSSF53732; Aconitase_N; 1; .
TIGRFAMsTIGR00117; AcnB; 1; .
PROSITEPS00450; ACONITASE_1; 1; .
PROSITEPS01244; ACONITASE_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