ID   ODO1_SOLTU              Reviewed;          19 AA.
AC   P81895;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2000, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial;
DE            EC=1.2.4.2;
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1;
DE            Short=OGDC-E1;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
DE   Flags: Fragment;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Romano {ECO:0000269|PubMed:10510296};
RC   TISSUE=Tuber {ECO:0000269|PubMed:10510296};
RX   PubMed=10510296; DOI=10.1042/0264-6021:3430327;
RA   Millar A.H., Hill S.A., Leaver C.J.;
RT   "Plant mitochondrial 2-oxoglutarate dehydrogenase complex: purification and
RT   characterization in potato.";
RL   Biochem. J. 343:327-334(1999).
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-oxoglutarate
CC       dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC       lipoamide dehydrogenase (E3). {ECO:0000269|PubMed:10510296}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC         COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000269|PubMed:10510296};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P20967};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000269|PubMed:10510296}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000305}.
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DR   PRIDE; P81895; -.
DR   BRENDA; 1.2.1.105; 5757.
DR   SABIO-RK; P81895; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IDA:UniProtKB.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; IDA:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Membrane; Mitochondrion;
KW   Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..>19
FT                   /note="2-oxoglutarate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000238928"
FT   NON_TER         19
FT                   /evidence="ECO:0000303|PubMed:10510296"
SQ   SEQUENCE   19 AA;  2024 MW;  3AB2C6910C61EEF7 CRC64;
     AQAAPVPRPV XLSKKTDSF