ID   ODPB_SOLTU              Reviewed;          16 AA.
AC   P81419;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1;
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)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC         acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   AlphaFoldDB; P81419; -.
DR   SABIO-RK; P81419; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Pyruvate; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..>16
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000162217"
FT   NON_TER         16
SQ   SEQUENCE   16 AA;  1705 MW;  FF6ED80EC804F797 CRC64;
     ISAVKEMTVR DALNSA