ID   ODPA_SOLTU              Reviewed;         391 AA.
AC   P52903;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=7659754; DOI=10.1104/pp.108.4.1623;
RA   Grof C.P., Winning B.M., Scaysbrook T.P., Hill S.A., Leaver C.J.;
RT   "Mitochondrial pyruvate dehydrogenase. Molecular cloning of the E1 alpha
RT   subunit and expression analysis.";
RL   Plant Physiol. 108:1623-1629(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44;
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [3]
RP   PROTEIN SEQUENCE OF 27-42.
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   -!- ACTIVITY REGULATION: E1 activity is regulated by phosphorylation
CC       (inactivation) and dephosphorylation (activation) of the alpha subunit.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z26949; CAA81558.1; -; mRNA.
DR   PIR; T07372; T07372.
DR   AlphaFoldDB; P52903; -.
DR   SMR; P52903; -.
DR   IntAct; P52903; 1.
DR   STRING; 4113.PGSC0003DMT400058223; -.
DR   iPTMnet; P52903; -.
DR   ProMEX; P52903; -.
DR   EnsemblPlants; PGSC0003DMT400058223; PGSC0003DMT400058223; PGSC0003DMG400022607.
DR   Gramene; PGSC0003DMT400058223; PGSC0003DMT400058223; PGSC0003DMG400022607.
DR   eggNOG; KOG0225; Eukaryota.
DR   HOGENOM; CLU_029393_5_0_1; -.
DR   InParanoid; P52903; -.
DR   OMA; FGMPGVT; -.
DR   BRENDA; 1.2.1.104; 5757.
DR   SABIO-RK; P52903; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P52903; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Pyruvate; Reference proteome; Thiamine pyrophosphate;
KW   Transit peptide.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:9729464"
FT   CHAIN           27..391
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha,
FT                   mitochondrial"
FT                   /id="PRO_0000020455"
FT   REGION          294..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  43228 MW;  F9110B374B022F0D CRC64;
     MALSTSRAIN HIMKPLSAAV CATRRLSSDS TATITVETSL PFTSHNIDPP SRSVETSPKE
     LMTFFKDMTE MRRMEIAADS LYKAKLIRGF CHLYDGQEAV AVGMEAAITK KDCIITAYRD
     HCIFLGRGGT LVEAFAELMG RRDGCSRGKG GSMHFYKKES GFYGGHGIVG AQVPLGIGLA
     FAQKYKKEDY VTFAMYGDGA ANQGQLFEAL NMAALWDLPA ILVCENNHYG MGTAEWRAAK
     SPAYYKRGDY VPGLRVDGMD VFAVKQACTF AKQHALKNGP IILEMDTYRY HGHSMSDPGS
     TYRTRDEISG VRQERDPVER IRSLILAHNI ATEAELKDIE KENRKVVDEA IAKAKESPMP
     DPSELFTNVY VKGFGVEAYG ADRKELRATL P