ID   ODP2_SOLTU              Reviewed;          21 AA.
AC   P81421;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=78 kDa dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
DE            EC=2.3.1.12;
DE   AltName: Full=78 kDa dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE   AltName: Full=Pyruvate dehydrogenase complex component E2 1;
DE            Short=PDC-E2 1;
DE            Short=PDCE2 1;
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]
RP   PROTEIN SEQUENCE.
RC   STRAIN=cv. Romano; TISSUE=Tuber;
RX   PubMed=9729464; DOI=10.1042/bj3340571;
RA   Millar A.H., Knorpp C., Leaver C.J., Hill S.A.;
RT   "Plant mitochondrial pyruvate dehydrogenase complex: purification and
RT   identification of catalytic components in potato.";
RL   Biochem. J. 334:571-576(1998).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC         N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83111; EC=2.3.1.12;
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 2 lipoyl cofactors covalently. {ECO:0000250};
CC   -!- SUBUNIT: Forms a 60-polypeptide structural core. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P81421; -.
DR   SABIO-RK; P81421; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Glycolysis; Lipoyl;
KW   Mitochondrion; Reference proteome; Transferase.
FT   CHAIN           1..>21
FT                   /note="78 kDa dihydrolipoyllysine-residue acetyltransferase
FT                   component of pyruvate dehydrogenase complex"
FT                   /id="PRO_0000162299"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2150 MW;  42BF35B23BB0FEFE CRC64;
     ISAEAPLYAE VGMPALSPTM T