ODP22_ARATH
ID ODP22_ARATH Reviewed; 539 AA.
AC Q8RWN9; Q9ASS8; Q9LVK7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial;
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide S-acetyltransferase component 2 of pyruvate dehydrogenase complex;
DE AltName: Full=Pyruvate dehydrogenase complex component E2 2;
DE Short=PDC-E2 2;
DE Short=PDCE2 2;
DE Flags: Precursor;
GN OrderedLocusNames=At3g13930; ORFNames=MDC16.5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [3]
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 [4]
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 [5]
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-102.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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 1 lipoyl cofactor covalently.;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02323.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019229; BAB02323.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75442.1; -; Genomic_DNA.
DR EMBL; AF367302; AAK32889.1; -; mRNA.
DR EMBL; AY091691; AAM10290.1; -; mRNA.
DR EMBL; AY092968; AAM12967.1; -; mRNA.
DR EMBL; BT000444; AAN17421.1; -; mRNA.
DR EMBL; BT000702; AAN31846.1; -; mRNA.
DR EMBL; BT001223; AAN65110.1; -; mRNA.
DR RefSeq; NP_566470.1; NM_112247.3.
DR AlphaFoldDB; Q8RWN9; -.
DR SMR; Q8RWN9; -.
DR BioGRID; 5940; 13.
DR STRING; 3702.AT3G13930.1; -.
DR iPTMnet; Q8RWN9; -.
DR PaxDb; Q8RWN9; -.
DR PRIDE; Q8RWN9; -.
DR ProteomicsDB; 250780; -.
DR EnsemblPlants; AT3G13930.1; AT3G13930.1; AT3G13930.
DR GeneID; 820606; -.
DR Gramene; AT3G13930.1; AT3G13930.1; AT3G13930.
DR KEGG; ath:AT3G13930; -.
DR Araport; AT3G13930; -.
DR TAIR; locus:2088247; AT3G13930.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; Q8RWN9; -.
DR OMA; DYLAKGC; -.
DR OrthoDB; 747232at2759; -.
DR PhylomeDB; Q8RWN9; -.
DR BioCyc; ARA:AT3G13930-MON; -.
DR BRENDA; 1.2.1.104; 399.
DR PRO; PR:Q8RWN9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RWN9; baseline and differential.
DR Genevisible; Q8RWN9; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
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; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Glycolysis; Lipoyl; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..102
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 103..539
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component 2 of pyruvate dehydrogenase complex,
FT mitochondrial"
FT /id="PRO_0000260026"
FT DOMAIN 111..187
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 248..285
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 102..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 512
FT /evidence="ECO:0000255"
FT ACT_SITE 516
FT /evidence="ECO:0000255"
FT MOD_RES 152
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 124
FT /note="T -> A (in Ref. 3; AAM12967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 58468 MW; 219B4BE0E7ACD05A CRC64;
MASRIINHSK KLKHVSALLR RDHAVAVRCF SNSTHPSLVG REDIFKARLN YSSVERISKC
GTGNVTMLSG ISTTSTKLSS PMAGPKLFKE FISSQMRSVR GFSSSSDLPP HQEIGMPSLS
PTMTEGNIAR WLKKEGDKVA PGEVLCEVET DKATVEMECM EEGFLAKIVK EEGAKEIQVG
EVIAITVEDE DDIQKFKDYT PSSDTGPAAP EAKPAPSLPK EEKVEKPASA PEAKISKPSS
APSEDRIFAS PLARKLAEDN NVPLSSIKGT GPEGRIVKAD VEDFLASGSK ETTAKPSKQV
DSKVPALDYV DIPHTQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKMMGLR SQLNSFQEAS
GGKRISVNDL VIKAAALALR KVPQCNSSWT DEYIRQFKNV NINVAVQTEN GLYVPVVKDA
DKKGLSTIGE EVRFLAQKAK ENSLKPEDYE GGTFTVSNLG GPFGIKQFCA VINPPQAAIL
AIGSAEKRVV PGTGPDQYNV ASYMSVTLSC DHRVIDGAIG AEWLKAFKGY IETPESMLL
