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   27-MAR-2024, entry version 168.
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   Name=E1 ALPHA; OrderedLocusNames=At1g59900; ORFNames=F23H11.21;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   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 deduced
RT   amino-acid sequences of a cDNA encoding the Arabidopsis thaliana E1 alpha-
RT   subunit.";
RL   Gene 164:251-254(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., 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., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
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 highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [7]
RP   INDUCTION BY CADMIUM.
RC   STRAIN=cv. Columbia;
RX   PubMed=16502469; DOI=10.1002/pmic.200500543;
RA   Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA   Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA   Ezan E., Garin J., Bourguignon J.;
RT   "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT   explored by protein and metabolite profiling analyses.";
RL   Proteomics 6:2180-2198(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
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=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC         acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase]; 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       {ECO:0000269|PubMed:14671022}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, rosettes and flowers.
CC       {ECO:0000269|PubMed:7590338}.
CC   -!- INDUCTION: Induced by cadmium. {ECO:0000269|PubMed:16502469}.
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DR   EMBL; U21214; AAA86507.1; -; mRNA.
DR   EMBL; AC007258; AAD39331.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33638.1; -; 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; NM_104682.3.
DR   AlphaFoldDB; P52901; -.
DR   SMR; P52901; -.
DR   BioGRID; 27509; 7.
DR   IntAct; P52901; 1.
DR   STRING; 3702.P52901; -.
DR   iPTMnet; P52901; -.
DR   MetOSite; P52901; -.
DR   PaxDb; 3702-AT1G59900-1; -.
DR   ProteomicsDB; 250787; -.
DR   EnsemblPlants; AT1G59900.1; AT1G59900.1; AT1G59900.
DR   GeneID; 842284; -.
DR   Gramene; AT1G59900.1; AT1G59900.1; AT1G59900.
DR   KEGG; ath:AT1G59900; -.
DR   Araport; AT1G59900; -.
DR   TAIR; AT1G59900; E1 ALPHA.
DR   eggNOG; KOG0225; Eukaryota.
DR   HOGENOM; CLU_029393_5_0_1; -.
DR   InParanoid; P52901; -.
DR   OrthoDB; 166915at2759; -.
DR   PhylomeDB; P52901; -.
DR   BioCyc; ARA:AT1G59900-MONOMER; -.
DR   PRO; PR:P52901; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P52901; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03182; PDH_E1_alph_y; 1.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SWISS-2DPAGE; P52901; -.
DR   Genevisible; P52901; AT.
PE   1: Evidence at protein level;
KW   Mitochondrion; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..389
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha-1,
FT                   mitochondrial"
FT                   /id="PRO_0000020453"
FT   CONFLICT        83..84
FT                   /note="KL -> NV (in Ref. 1; AAA86507)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        362
FT                   /note="E -> D (in Ref. 4; AAK26016)"
FT                   /evidence="ECO:0000305"
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
//