ID   ODPA2_ARATH             Reviewed;         393 AA.
AC   Q8H1Y0; O48685;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   AltName: Full=Protein IAA-CONJUGATE-RESISTANT 4;
DE   Flags: Precursor;
GN   Name=IAR4; OrderedLocusNames=At1g24180; ORFNames=F3I6.11;
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], MUTAGENESIS OF ARG-121, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=15173569; DOI=10.1104/pp.104.040519;
RA   LeClere S., Rampey R.A., Bartel B.;
RT   "IAR4, a gene required for auxin conjugate sensitivity in Arabidopsis,
RT   encodes a pyruvate dehydrogenase E1alpha homolog.";
RL   Plant Physiol. 135:989-999(2004).
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).
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       {ECO:0000269|PubMed:14671022}.
CC   -!- DISRUPTION PHENOTYPE: Reduced sensitivity to several IAA-amino acid
CC       conjugates. {ECO:0000269|PubMed:15173569}.
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DR   EMBL; AY135561; AAN15218.1; -; mRNA.
DR   EMBL; AC002396; AAC00577.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30492.1; -; Genomic_DNA.
DR   EMBL; AF360215; AAK25925.1; -; mRNA.
DR   EMBL; AY051018; AAK93695.1; -; mRNA.
DR   EMBL; AY088101; AAM65647.1; -; mRNA.
DR   PIR; T00648; T00648.
DR   RefSeq; NP_173828.1; NM_102264.5.
DR   AlphaFoldDB; Q8H1Y0; -.
DR   SMR; Q8H1Y0; -.
DR   BioGRID; 24269; 10.
DR   STRING; 3702.AT1G24180.1; -.
DR   iPTMnet; Q8H1Y0; -.
DR   PaxDb; Q8H1Y0; -.
DR   PRIDE; Q8H1Y0; -.
DR   ProteomicsDB; 250957; -.
DR   EnsemblPlants; AT1G24180.1; AT1G24180.1; AT1G24180.
DR   GeneID; 839031; -.
DR   Gramene; AT1G24180.1; AT1G24180.1; AT1G24180.
DR   KEGG; ath:AT1G24180; -.
DR   Araport; AT1G24180; -.
DR   TAIR; locus:2032367; AT1G24180.
DR   eggNOG; KOG0225; Eukaryota.
DR   HOGENOM; CLU_029393_5_2_1; -.
DR   InParanoid; Q8H1Y0; -.
DR   OMA; YRSHGFT; -.
DR   OrthoDB; 871160at2759; -.
DR   PhylomeDB; Q8H1Y0; -.
DR   BioCyc; ARA:AT1G24180-MON; -.
DR   PRO; PR:Q8H1Y0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8H1Y0; baseline and differential.
DR   Genevisible; Q8H1Y0; AT.
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:0050897; F:cobalt ion binding; HDA:TAIR.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
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   Glycolysis; Mitochondrion; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..393
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha-2,
FT                   mitochondrial"
FT                   /id="PRO_0000260024"
FT   MUTAGEN         121
FT                   /note="R->C: In iar4-1; reduced sensitivity to several IAA-
FT                   amino acid conjugates."
FT                   /evidence="ECO:0000269|PubMed:15173569"
FT   CONFLICT        231
FT                   /note="Y -> D (in Ref. 1; AAN15218)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  43359 MW;  1B28971865B52817 CRC64;
     MALSRLSSRS NTFLKPAITA LPSSIRRHVS TDSSPITIET AVPFTSHLCE SPSRSVETSS
     EEILAFFRDM ARMRRMEIAA DSLYKAKLIR GFCHLYDGQE ALAVGMEAAI TKKDAIITSY
     RDHCTFIGRG GKLVDAFSEL MGRKTGCSHG KGGSMHFYKK DASFYGGHGI VGAQIPLGCG
     LAFAQKYNKD EAVTFALYGD GAANQGQLFE ALNISALWDL PAILVCENNH YGMGTATWRS
     AKSPAYFKRG DYVPGLKVDG MDALAVKQAC KFAKEHALKN GPIILEMDTY RYHGHSMSDP
     GSTYRTRDEI SGVRQVRDPI ERVRKLLLTH DIATEKELKD MEKEIRKEVD DAVAQAKESP
     IPDASELFTN MYVKDCGVES FGADRKELKV TLP