ID   ODPA1_ARATH             Reviewed;         389 AA.
AC   P52901; Q9C5E3; Q9SXC2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   16-DEC-2008, entry version 75.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g59900; ORFNames=F23H11.21;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=96069590; PubMed=7590338; DOI=10.1016/0378-1119(95)00465-I;
RA   Luethy M.H., Miernyk J.A., Randall D.D.;
RT   "The mitochondrial pyruvate dehydrogenase complex: nucleotide and
RT   deduced amino-acid sequences of a cDNA encoding the Arabidopsis
RT   thaliana E1 alpha-subunit.";
RL   Gene 164:251-254(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome
RT   highlights signaling and regulatory components, provides assessment of
RT   targeting prediction programs, and indicates plant-specific
RT   mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
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; U21214; AAA86507.1; -; mRNA.
DR   EMBL; AC007258; AAD39331.1; -; Genomic_DNA.
DR   EMBL; AF360306; AAK26016.1; -; mRNA.
DR   EMBL; BT000974; AAN41374.1; -; mRNA.
DR   EMBL; AY087667; AAM65205.1; -; mRNA.
DR   PIR; B96623; B96623.
DR   PIR; JC4358; JC4358.
DR   RefSeq; NP_176198.1; -.
DR   UniGene; At.23186; -.
DR   HSSP; P08559; 1NI4.
DR   SWISS-2DPAGE; P52901; -.
DR   PRIDE; P52901; -.
DR   GeneID; 842284; -.
DR   GenomeReviews; CT485782_GR; AT1G59900.
DR   KEGG; ath:AT1G59900; -.
DR   NMPDR; fig|3702.1.peg.5381; -.
DR   GeneFarm; 4372; 441.
DR   TAIR; At1g59900; -.
DR   ArrayExpress; P52901; -.
DR   GermOnline; AT1G59900; Arabidopsis thaliana.
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   GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR   InterPro; IPR001017; DHase_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   Pfam; PF00676; E1_dh; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1     32       Mitochondrion (Potential).
FT   CHAIN        33    389       Pyruvate dehydrogenase E1 component
FT                                subunit alpha-1, mitochondrial.
FT                                /FTId=PRO_0000020453.
FT   CONFLICT     83     84       KL -> NV (in Ref. 1; AAA86507).
FT   CONFLICT    362    362       E -> D (in Ref. 3; AAK26016).
SQ   SEQUENCE   389 AA;  43059 MW;  637E5BE5E86DCCAE CRC64;
     MALSRLSSRS NIITRPFSAA FSRLISTDTT PITIETSLPF TAHLCDPPSR SVESSSQELL
     DFFRTMALMR RMEIAADSLY KAKLIRGFCH LYDGQEAVAI GMEAAITKKD AIITAYRDHC
     IFLGRGGSLH EVFSELMGRQ AGCSKGKGGS MHFYKKESSF YGGHGIVGAQ VPLGCGIAFA
     QKYNKEEAVT FALYGDGAAN QGQLFEALNI SALWDLPAIL VCENNHYGMG TAEWRAAKSP
     SYYKRGDYVP GLKVDGMDAF AVKQACKFAK QHALEKGPII LEMDTYRYHG HSMSDPGSTY
     RTRDEISGVR QERDPIERIK KLVLSHDLAT EKELKDMEKE IRKEVDDAIA KAKDCPMPEP
     SELFTNVYVK GFGTESFGPD RKEVKASLP
//