ID   ODP3_SOLTU              Reviewed;          15 AA.
AC   P81420;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=55 kDa dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
DE            EC=2.3.1.12;
DE   AltName: Full=55 kDa dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE   AltName: Full=Pyruvate dehydrogenase complex component E2 2;
DE            Short=PDC-E2 2;
DE            Short=PDCE2 2;
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=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC         + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
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 1 lipoyl cofactor covalently. {ECO:0000250};
CC   -!- SUBUNIT: Forms a 60-polypeptide structural core. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   InParanoid; P81420; -.
DR   SABIO-RK; P81420; -.
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; Lipoyl; Mitochondrion;
KW   Reference proteome; Transferase.
FT   CHAIN           1..>15
FT                   /note="55 kDa dihydrolipoyllysine-residue acetyltransferase
FT                   component of pyruvate dehydrogenase complex"
FT                   /id="PRO_0000162300"
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1449 MW;  EA28B063799BE825 CRC64;
     SSADSLPXHG AGXMP
//