ID   ODO2_SOLTU              Reviewed;          20 AA.
AC   P81896;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2000, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Dihydrolipoamide-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE            EC=2.3.1.61;
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE            Short=OGDC-E2;
DE   AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE   AltName: Full=E2K;
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)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
CC         Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000269|PubMed:10510296};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000250|UniProtKB:Q01205};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000250|UniProtKB:Q01205};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 6/6.
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000250|UniProtKB:Q01205}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000269|PubMed:10510296}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000255}.
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DR   STRING; 4113.PGSC0003DMT400071652; -.
DR   eggNOG; KOG0559; Eukaryota.
DR   BRENDA; 1.2.1.105; 5757.
DR   SABIO-RK; P81896; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Lipoyl; Membrane;
KW   Mitochondrion; Reference proteome; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..>20
FT                   /note="Dihydrolipoamide-residue succinyltransferase
FT                   component of 2-oxoglutarate dehydrogenase complex"
FT                   /id="PRO_0000238929"
FT   NON_TER         20
FT                   /evidence="ECO:0000303|PubMed:10510296"
SQ   SEQUENCE   20 AA;  2051 MW;  9256BE292E26A344 CRC64;
     XSNSGDLVDA VVPYMGESIS