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   27-MAR-2024, entry version 126.
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=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC         + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
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   STRING; 3702.Q0WQF7; -.
DR   SwissPalm; 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   TAIR; AT3G52200; LTA3.
DR   eggNOG; KOG0557; Eukaryota.
DR   HOGENOM; CLU_016733_10_2_1; -.
DR   InParanoid; Q0WQF7; -.
DR   OMA; TIKQKPW; -.
DR   PhylomeDB; Q0WQF7; -.
DR   BioCyc; ARA:AT3G52200-MONOMER; -.
DR   BRENDA; 1.2.1.104; 399.
DR   PRO; PR:Q0WQF7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q0WQF7; baseline and differential.
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   CDD; cd06849; lipoyl_domain; 2.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 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; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF9; PYRUVATE DEHYDROGENASE PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
DR   Genevisible; Q0WQF7; AT.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; 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
//