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 16-JUN-2009, entry version 41. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial; DE Short=PDHE1-A; DE EC=1.2.4.1; 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; 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 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 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY135561; AAN15218.1; -; mRNA. DR EMBL; AE005172; AAC00577.1; -; Genomic_DNA. DR EMBL; AF360215; AAK25925.1; -; mRNA. DR EMBL; AY051018; AAK93695.1; -; mRNA. DR EMBL; AY088101; AAM65647.1; -; mRNA. DR IPI; IPI00540928; -. DR PIR; T00648; T00648. DR RefSeq; NP_173828.1; -. DR UniGene; At.24830; -. DR HSSP; P08559; 1NI4. DR PRIDE; Q8H1Y0; -. DR ProMEX; Q8H1Y0; -. DR GeneID; 839031; -. DR GenomeReviews; CT485782_GR; AT1G24180. DR KEGG; ath:AT1G24180; -. DR NMPDR; fig|3702.1.peg.2808; -. DR GeneFarm; 4373; 441. DR TAIR; At1g24180; -. DR OMA; Q8H1Y0; TAYRCHA. DR BRENDA; 1.2.4.1; 302. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:TAIR. 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:0009651; P:response to salt stress; IEP:TAIR. 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 Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase; KW Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide. FT TRANSIT 1 28 Mitochondrion (Potential). FT CHAIN 29 393 Pyruvate dehydrogenase E1 component FT subunit alpha-2, mitochondrial. FT /FTId=PRO_0000260024. FT CONFLICT 231 231 Y -> D (in Ref. 1; AAN15218). 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 //