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UniProtKB/Swiss-Prot entry P0AFG3

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODO1_ECOLI
Primary accession number P0AFG3
Secondary accession numbers P07015 P78225
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on December 20, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 31)
Name and origin of the protein
Protein name 2-oxoglutarate dehydrogenase E1 component
Synonyms EC 1.2.4.2
Alpha-ketoglutarate dehydrogenase
Gene name
Name: sucA
OrderedLocusNames: b0726, JW0715
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6376123 [NCBI, ExPASy, EBI, Israel, Japan]
Darlison M.G., Spencer M.E., Guest J.R.;
"Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12.";
Eur. J. Biochem. 141:351-359(1984).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
Comments
  • FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
  • CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • SUBUNIT: Homodimer.
  • SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J01619; AAA23897.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00661; CAA25280.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73820.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35392.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E64808; DEECOG.
RefSeq AP_001363.1; -.
NP_415254.1; -.
3D structure databases
PDB
2JGD; X-ray; 2.60 A; A/B=1-933.[ExPASy / RCSB / EBI]
PDBsum 2JGD; -.
ModBase P0AFG3.
Protein-protein interaction databases
IntAct P0AFG3; 15.
Enzyme and pathway databases
BioCyc EcoCyc:E1O-MON; -.
MetaCyc:E1O-MON; -.
2D gel databases
SWISS-2DPAGE P0AFG3; -.
ECO2DBASE G097.0; 6TH EDITION.
Organism-specific databases
EchoBASE EB0972; -.
EcoGene EG10979; sucA.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0004591; Molecular function: oxoglutarate dehydrogenase (succinyl-transferring) activity (inferred from electronic annotation from InterPro).
GO:0030976; Molecular function: thiamin pyrophosphate binding (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR011603; 2oxoglutarate_DHase_E1.
IPR001017; DHase_E1.
IPR005475; Transketo_Cen_R.
Graphical view of domain structure.
PANTHER PTHR23152; 2oxoglutarate_DH_E1; 1.
Pfam PF00676; E1_dh; 1.
PF02779; Transket_pyr; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000157; Oxoglu_dh_E1; 1.
TIGRFAMs TIGR00239; 2oxo_dh_E1; 1.
Genome annotation databases
GeneID 945303; -.
GenomeReviews AP009048_GR; JW0715.
U00096_GR; b0726.
KEGG ecj:JW0715; -.
eco:b0726; -.
Phylogenomic databases
HOGENOM P0AFG3; -.
Genome annotation databases
CMR P0AFG3; b0726.
Other
ProtoNet P0AFG3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   933  933     2-oxoglutarate dehydrogenase E1 component. PRO_0000162191
CONFLICT   454   454        C -> S (in Ref. 1; AAA23897/CAA25280). 
HELIX   85   102  18      
HELIX   103   106  4      
STRAND   111   113  3      
HELIX   126   129  4      
STRAND   137   140  4      
STRAND   150   152  3      
HELIX   153   165  13      
STRAND   166   171  6      
HELIX   178   188  11      
HELIX   197   220  24      
HELIX   235   247  13      
TURN   248   250  3      
STRAND   253   257  5      
HELIX   263   269  7      
HELIX   275   282  8      
HELIX   296   298  3      
STRAND   301   307  7      
STRAND   310   316  7      
HELIX   326   338  13      
STRAND   341   343  3      
HELIX   346   348  3      
STRAND   349   356  8      
HELIX   357   362  6      
HELIX   365   372  8      
TURN   376   378  3      
STRAND   384   389  6      
HELIX   408   413  6      
TURN   414   416  3      
STRAND   419   423  5      
HELIX   427   444  18      
STRAND   448   453  6      
HELIX   474   478  5      
HELIX   483   492  10      
TURN   493   495  3      
HELIX   499   515  17      
HELIX   528   530  3      
HELIX   534   536  3      
HELIX   551   560  10      
HELIX   572   585  14      
HELIX   593   605  13      
TURN   606   608  3      
STRAND   611   615  5      
TURN   616   620  5      
STRAND   629   631  3      
STRAND   633   636  4      
HELIX   641   643  3      
STRAND   652   655  4      
HELIX   661   674  14      
STRAND   678   683  6      
HELIX   687   693  7      
HELIX   694   699  6      
TURN   700   703  4      
HELIX   704   708  5      
STRAND   715   719  5      
STRAND   723   725  3      
HELIX   734   739  6      
STRAND   747   749  3      
HELIX   754   766  13      
STRAND   773   777  5      
HELIX   780   783  4      
HELIX   791   796  6      
STRAND   801   803  3      
HELIX   811   813  3      
STRAND   816   820  5      
HELIX   824   834  11      
STRAND   839   845  7      
STRAND   847   850  4      
HELIX   853   860  8      
HELIX   861   863  3      
STRAND   868   876  9      
HELIX   882   890  9      
STRAND   898   904  7      
STRAND   908   911  4      
HELIX   915   930  16      
Sequence information
Length: 933 AA [This is the length of the unprocessed precursor] Molecular weight: 105062 Da [This is the MW of the unprocessed precursor] CRC64: EAEF8429EC31E749 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQNSALKAWL DSSYLSGANQ SWIEQLYEDF LTDPDSVDAN WRSTFQQLPG TGVKPDQFHS 

        70         80         90        100        110        120 
QTREYFRRLA KDASRYSSTI SDPDTNVKQV KVLQLINAYR FRGHQHANLD PLGLWQQDKV 

       130        140        150        160        170        180 
ADLDPSFHDL TEADFQETFN VGSFASGKET MKLGELLEAL KQTYCGPIGA EYMHITSTEE 

       190        200        210        220        230        240 
KRWIQQRIES GRATFNSEEK KRFLSELTAA EGLERYLGAK FPGAKRFSLE GGDALIPMLK 

       250        260        270        280        290        300 
EMIRHAGNSG TREVVLGMAH RGRLNVLVNV LGKKPQDLFD EFAGKHKEHL GTGDVKYHMG 

       310        320        330        340        350        360 
FSSDFQTDGG LVHLALAFNP SHLEIVSPVV IGSVRARLDR LDEPSSNKVL PITIHGDAAV 

       370        380        390        400        410        420 
TGQGVVQETL NMSKARGYEV GGTVRIVINN QVGFTTSNPL DARSTPYCTD IGKMVQAPIF 

       430        440        450        460        470        480 
HVNADDPEAV AFVTRLALDF RNTFKRDVFI DLVCYRRHGH NEADEPSATQ PLMYQKIKKH 

       490        500        510        520        530        540 
PTPRKIYADK LEQEKVATLE DATEMVNLYR DALDAGDCVV AEWRPMNMHS FTWSPYLNHE 

       550        560        570        580        590        600 
WDEEYPNKVE MKRLQELAKR ISTVPEAVEM QSRVAKIYGD RQAMAAGEKL FDWGGAENLA 

       610        620        630        640        650        660 
YATLVDEGIP VRLSGEDSGR GTFFHRHAVI HNQSNGSTYT PLQHIHNGQG AFRVWDSVLS 

       670        680        690        700        710        720 
EEAVLAFEYG YATAEPRTLT IWEAQFGDFA NGAQVVIDQF ISSGEQKWGR MCGLVMLLPH 

       730        740        750        760        770        780 
GYEGQGPEHS SARLERYLQL CAEQNMQVCV PSTPAQVYHM LRRQALRGMR RPLVVMSPKS 

       790        800        810        820        830        840 
LLRHPLAVSS LEELANGTFL PAIGEIDELD PKGVKRVVMC SGKVYYDLLE QRRKNNQHDV 

       850        860        870        880        890        900 
AIVRIEQLYP FPHKAMQEVL QQFAHVKDFV WCQEEPLNQG AWYCSQHHFR EVIPFGASLR 

       910        920        930 
YAGRPASASP AVGYMSVHQK QQQDLVNDAL NVE
P0AFG3 in FASTA format

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