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   16-JUN-2009, entry version 60.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   MEDLINE=95388769; 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
RT   alpha subunit and expression analysis.";
RL   Plant Physiol. 108:1623-1629(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-42.
RC   STRAIN=cv. Romano; TISSUE=Tuber;
RX   MEDLINE=98399821; PubMed=9729464;
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
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate.
CC   -!- ENZYME REGULATION: E1 activity is regulated by phosphorylation
CC       (inactivation) and dephosphorylation (activation) of the alpha
CC       subunit (By similarity).
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   EMBL; Z26949; CAA81558.1; -; mRNA.
DR   PIR; T07372; T07372.
DR   HSSP; P08559; 1NI4.
DR   IntAct; P52903; 1.
DR   BRENDA; 1.2.4.1; 296.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   Pfam; PF00676; E1_dh; 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; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1     26       Mitochondrion.
FT   CHAIN        27    391       Pyruvate dehydrogenase E1 component
FT                                subunit alpha, mitochondrial.
FT                                /FTId=PRO_0000020455.
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
//