ODP21_ARATH
ID ODP21_ARATH Reviewed; 637 AA.
AC Q0WQF7; Q39082; Q9SQI7; Q9SUY5;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial;
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide S-acetyltransferase component 1 of pyruvate dehydrogenase complex;
DE AltName: Full=Pyruvate dehydrogenase complex component E2 1;
DE Short=PDC-E2 1;
DE Short=PDCE2 1;
DE Flags: Precursor;
GN Name=LTA3; OrderedLocusNames=At3g52200; ORFNames=F4F15.310;
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].
RA Mooney B.P., Miernyk J.A., Randall D.D.;
RT "Expression and assembly of the mitochondrial dihydrolipoamide S-
RT acetyltransferase (E2) subunit from Arabidopsis thaliana.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-637.
RX PubMed=7890655; DOI=10.1074/jbc.270.10.5412;
RA Guan Y., Rawsthorne S., Scofield G., Shaw P., Doonan J.H.;
RT "Cloning and characterization of a dihydrolipoamide acetyltransferase (E2)
RT subunit of the pyruvate dehydrogenase complex from Arabidopsis thaliana.";
RL J. Biol. Chem. 270:5412-5417(1995).
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 FUNCTION.
RX PubMed=14764908; DOI=10.1104/pp.103.035675;
RA Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.;
RT "Lipoic acid-dependent oxidative catabolism of alpha-keto acids in
RT mitochondria provides evidence for branched-chain amino acid catabolism in
RT Arabidopsis.";
RL Plant Physiol. 134:838-848(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). {ECO:0000269|PubMed:14764908}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Note=Binds 2 lipoyl cofactors covalently.;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14671022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q0WQF7-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF066080; AAD55140.1; -; mRNA.
DR EMBL; AL049711; CAB41340.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78912.1; -; Genomic_DNA.
DR EMBL; AK228742; BAF00642.1; -; mRNA.
DR EMBL; Z46230; CAA86300.1; -; mRNA.
DR PIR; A55939; A55939.
DR PIR; T49099; T49099.
DR RefSeq; NP_190788.1; NM_115080.3. [Q0WQF7-1]
DR AlphaFoldDB; Q0WQF7; -.
DR SMR; Q0WQF7; -.
DR BioGRID; 9703; 14.
DR SwissPalm; Q0WQF7; -.
DR PaxDb; Q0WQF7; -.
DR PRIDE; Q0WQF7; -.
DR ProteomicsDB; 239003; -. [Q0WQF7-1]
DR EnsemblPlants; AT3G52200.1; AT3G52200.1; AT3G52200. [Q0WQF7-1]
DR GeneID; 824385; -.
DR Gramene; AT3G52200.1; AT3G52200.1; AT3G52200. [Q0WQF7-1]
DR KEGG; ath:AT3G52200; -.
DR Araport; AT3G52200; -.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; Q0WQF7; -.
DR OMA; QVTVIKH; -.
DR PhylomeDB; Q0WQF7; -.
DR BioCyc; ARA:AT3G52200-MON; -.
DR BRENDA; 1.2.1.104; 399.
DR PRO; PR:Q0WQF7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WQF7; baseline and differential.
DR Genevisible; Q0WQF7; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase 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 Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; PTHR23151; 2.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Glycolysis; Lipoyl; Mitochondrion;
KW Reference proteome; Repeat; Transferase; Transit peptide.
FT TRANSIT 1..84
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 85..637
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component 1 of pyruvate dehydrogenase complex,
FT mitochondrial"
FT /id="PRO_0000260025"
FT DOMAIN 85..161
FT /note="Lipoyl-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 212..288
FT /note="Lipoyl-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 330..367
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 171..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 610
FT /evidence="ECO:0000255"
FT ACT_SITE 614
FT /evidence="ECO:0000255"
FT MOD_RES 126
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 253
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 6
FT /note="F -> L (in Ref. 4; BAF00642)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="S -> F (in Ref. 1; AAD55140)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="V -> E (in Ref. 1; AAD55140 and 5; CAA86300)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="S -> C (in Ref. 1; AAD55140 and 5; CAA86300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 68862 MW; CBD20C3B1BF2B4E9 CRC64;
MVLPLFRRAA IARTSSLLRA RLFAPASEFH SRFSNGLYHL DDKISSSNGV RSASIDLITR
MDDSSPKPIL RFGVQNFSST GPISQTVLAM PALSPTMSHG NVVKWMKKEG DKVEVGDVLC
EIETDKATVE FESQEEGFLA KILVTEGSKD IPVNEPIAIM VEEEDDIKNV PATIEGGRDG
KEETSAHQVM KPDESTQQKS SIQPDASDLP PHVVLEMPAL SPTMNQGNIA KWWKKEGDKI
EVGDVIGEIE TDKATLEFES LEEGYLAKIL IPEGSKDVAV GKPIALIVED AESIEAIKSS
SAGSSEVDTV KEVPDSVVDK PTERKAGFTK ISPAAKLLIL EHGLEASSIE ASGPYGTLLK
SDVVAAIASG KASKSSASTK KKQPSKETPS KSSSTSKPSV TQSDNNYEDF PNSQIRKIIA
KRLLESKQKI PHLYLQSDVV LDPLLAFRKE LQENHGVKVS VNDIVIKAVA VALRNVRQAN
AFWDAEKGDI VMCDSVDISI AVATEKGLMT PIIKNADQKS ISAISLEVKE LAQKARSGKL
APHEFQGGTF SISNLGMYPV DNFCAIINPP QAGILAVGRG NKVVEPVIGL DGIEKPSVVT
KMNVTLSADH RIFDGQVGAS FMSELRSNFE DVRRLLL
