ODPA3_ARATH
ID ODPA3_ARATH Reviewed; 428 AA.
AC O24457; Q9MAM6;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic;
DE EC=1.2.4.1;
DE Flags: Precursor;
GN Name=PDH-E1 ALPHA; OrderedLocusNames=At1g01090; ORFNames=T25K16.8;
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].
RC STRAIN=cv. Columbia;
RX PubMed=9393637; DOI=10.1016/s0005-2728(97)00059-5;
RA Johnston M.L., Luethy M.H., Miernyk J.A., Randall D.D.;
RT "Cloning and molecular analyses of the Arabidopsis thaliana plastid
RT pyruvate dehydrogenase subunits.";
RL Biochim. Biophys. Acta 1321:200-206(1997).
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). {ECO:0000250}.
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 Evidence={ECO:0000250};
CC -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26472.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g01080 and At1g01090.; Evidence={ECO:0000305};
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DR EMBL; U80185; AAB86803.1; -; mRNA.
DR EMBL; AC007323; AAF26472.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27233.1; -; Genomic_DNA.
DR EMBL; AY052721; AAK96625.1; -; mRNA.
DR EMBL; AY063724; AAL36074.1; -; mRNA.
DR EMBL; AK226909; BAE98984.1; -; mRNA.
DR RefSeq; NP_171617.1; NM_099991.4.
DR AlphaFoldDB; O24457; -.
DR SMR; O24457; -.
DR BioGRID; 24664; 9.
DR IntAct; O24457; 2.
DR STRING; 3702.AT1G01090.1; -.
DR PaxDb; O24457; -.
DR PRIDE; O24457; -.
DR ProMEX; O24457; -.
DR ProteomicsDB; 250788; -.
DR EnsemblPlants; AT1G01090.1; AT1G01090.1; AT1G01090.
DR GeneID; 839429; -.
DR Gramene; AT1G01090.1; AT1G01090.1; AT1G01090.
DR KEGG; ath:AT1G01090; -.
DR Araport; AT1G01090; -.
DR TAIR; locus:2200980; AT1G01090.
DR eggNOG; KOG0225; Eukaryota.
DR HOGENOM; CLU_029393_5_1_1; -.
DR InParanoid; O24457; -.
DR OMA; NDARAVY; -.
DR OrthoDB; 871160at2759; -.
DR PhylomeDB; O24457; -.
DR BioCyc; ARA:AT1G01090-MON; -.
DR PRO; PR:O24457; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O24457; baseline and differential.
DR Genevisible; O24457; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..428
FT /note="Pyruvate dehydrogenase E1 component subunit alpha-3,
FT chloroplastic"
FT /id="PRO_0000421367"
SQ SEQUENCE 428 AA; 47174 MW; 4A7A8D8BED2D2578 CRC64;
MATAFAPTKL TATVPLHGSH ENRLLLPIRL APPSSFLGST RSLSLRRLNH SNATRRSPVV
SVQEVVKEKQ STNNTSLLIT KEEGLELYED MILGRSFEDM CAQMYYRGKM FGFVHLYNGQ
EAVSTGFIKL LTKSDSVVST YRDHVHALSK GVSARAVMSE LFGKVTGCCR GQGGSMHMFS
KEHNMLGGFA FIGEGIPVAT GAAFSSKYRR EVLKQDCDDV TVAFFGDGTC NNGQFFECLN
MAALYKLPII FVVENNLWAI GMSHLRATSD PEIWKKGPAF GMPGVHVDGM DVLKVREVAK
EAVTRARRGE GPTLVECETY RFRGHSLADP DELRDAAEKA KYAARDPIAA LKKYLIENKL
AKEAELKSIE KKIDELVEEA VEFADASPQP GRSQLLENVF ADPKGFGIGP DGRYRCEDPK
FTEGTAQV
