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UniProtKB/Swiss-Prot entry P20707


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

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Entry information
Entry name ODO1_AZOVI
Primary accession number P20707
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on February 1, 1991 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 49)
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
Synonyms: odhA
From
Azotobacter vinelandii [TaxID: 354] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Azotobacter.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2404759 [NCBI, ExPASy, EBI, Israel, Japan]
Schulze E., Westphal A.H., Hanemaaijer R., de Kok A.;
"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component.";
Eur. J. Biochem. 187:229-234(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 909-943.
PubMed=2404760 [NCBI, ExPASy, EBI, Israel, Japan]
Westphal A.H., de Kok A.;
"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component.";
Eur. J. Biochem. 187:235-239(1990).
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
X52433; CAA36680.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52432; CAA36677.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S07776; S07776.
3D structure databases
ModBase P20707.
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.
BLOCKS P20707.
Other
ProtoNet P20707.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   943  943     2-oxoglutarate dehydrogenase E1 component. PRO_0000162186
Sequence information
Length: 943 AA [This is the length of the unprocessed precursor] Molecular weight: 105688 Da [This is the MW of the unprocessed precursor] CRC64: D3F35356D454E2A1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQDSVMQRMW NSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFEKLPA EAGTSTDVPH 

        70         80         90        100        110        120 
APVRDQFVLL AKNQRRAQPV ATSSVSTEHE KKQVEVLRLI QAYRTRGHQA SQLDPLGLWQ 

       130        140        150        160        170        180 
RTAPSDLSIT HYGLTNADLD TPFRTGELYI GKEEATLREI LQALQETYCR TIGAEFTHIV 

       190        200        210        220        230        240 
DSEQRNWFAQ RLESVRGRPV YSKEAKSHLL ERLSAAEGLE KYLGTKYPGT KRFGLEGGES 

       250        260        270        280        290        300 
LVPVVDEIIQ RSGSYGTKEV VIGMAHRGRL NLLVNALGKN PRDLFDEFEG KHLVELGSGD 

       310        320        330        340        350        360 
VKYHQGFSSN VMTSGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRVDA TGEKVVPISI 

       370        380        390        400        410        420 
HGDSAFAGQG VVMETFQMSQ IRGYKTGGTI HIVVNNQVGF TTSNPVDTRS TEYCTDPAKM 

       430        440        450        460        470        480 
IQAPVLHVNG DDPEAVLFVT QLAVDYRMQF KRDVVIDLVC YRRRGHNEAD EPSGTQPLMY 

       490        500        510        520        530        540 
QKIAKQPTTR ELYADALVKE GSLSQEEVQA KVDEYRTALD NGQHVLKSLV KEPNTELFVD 

       550        560        570        580        590        600 
WTPYLGHAWT ARHDTSFELK TLQELNAKLL QIPEGFVVQR QVAKILEDRG RMGVGAMPIN 

       610        620        630        640        650        660 
WGCAETLAYA TLLKEGHPVR ITGQDVGRGT FSHRHAALHN QKDASRYIPL QNLYEGQPKF 

       670        680        690        700        710        720 
ELYDSFLSEE AVLAFEYGYA TTTPNALVIW EASSGDFANG AQVVIDQFIS SGETKWGALC 

       730        740        750        760        770        780 
GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EQNIQVCVPT TPAQVYHMLR RQVIRPLRKP 

       790        800        810        820        830        840 
LVALTPKSLL RHKSAISTLE DLALGSFHPV LPEVDSLDPK KVERLVLCSG KVYYDLLDKR 

       850        860        870        880        890        900 
HAEGREDIAI VRIEQLYPFP EEELAEVMAP YTNLKHVVWC QEEPMNQGAW YCSQHHMRRV 

       910        920        930        940 
ASAHKKELFL QYAGREASAA PACGYASMHA EQQEKLLQDA FTV 

P20707 in FASTA format

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View entry in raw text format (no links)
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