ODP24_ARATH
ID ODP24_ARATH Reviewed; 480 AA.
AC Q9SQI8; Q9LUA6;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component 4 of pyruvate dehydrogenase complex, chloroplastic;
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide S-acetyltransferase component 4 of pyruvate dehydrogenase complex;
DE AltName: Full=Pyruvate dehydrogenase complex component E2 4;
DE Short=PDC-E2 4;
DE Short=PDCE2 4;
DE Short=plE2;
DE Flags: Precursor;
GN Name=LTA2; OrderedLocusNames=At3g25860; ORFNames=MPE11.1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10364395; DOI=10.1104/pp.120.2.443;
RA Mooney B.P., Miernyk J.A., Randall D.D.;
RT "Cloning and characterization of the dihydrolipoamide S-acetyltransferase
RT subunit of the plastid pyruvate dehydrogenase complex (E2) from
RT Arabidopsis.";
RL Plant Physiol. 120:443-452(1999).
RN [2]
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 [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 DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=13677473; DOI=10.1023/a:1025076805902;
RA Lin M., Behal R., Oliver D.J.;
RT "Disruption of plE2, the gene for the E2 subunit of the plastid pyruvate
RT dehydrogenase complex, in Arabidopsis causes an early embryo lethal
RT phenotype.";
RL Plant Mol. Biol. 52:865-872(2003).
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)-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; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:10364395}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:13677473}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01047.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF066079; AAD55139.1; -; mRNA.
DR EMBL; AB023041; BAB01047.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE77080.1; -; Genomic_DNA.
DR EMBL; AY037262; AAK59863.1; -; mRNA.
DR EMBL; BT002343; AAN86176.1; -; mRNA.
DR RefSeq; NP_189215.1; NM_113489.3.
DR AlphaFoldDB; Q9SQI8; -.
DR SMR; Q9SQI8; -.
DR BioGRID; 7512; 14.
DR IntAct; Q9SQI8; 4.
DR STRING; 3702.AT3G25860.1; -.
DR iPTMnet; Q9SQI8; -.
DR SwissPalm; Q9SQI8; -.
DR PaxDb; Q9SQI8; -.
DR PRIDE; Q9SQI8; -.
DR ProteomicsDB; 250782; -.
DR EnsemblPlants; AT3G25860.1; AT3G25860.1; AT3G25860.
DR GeneID; 822181; -.
DR Gramene; AT3G25860.1; AT3G25860.1; AT3G25860.
DR KEGG; ath:AT3G25860; -.
DR Araport; AT3G25860; -.
DR TAIR; locus:2092070; AT3G25860.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; Q9SQI8; -.
DR OMA; RAMAQNM; -.
DR OrthoDB; 747232at2759; -.
DR PhylomeDB; Q9SQI8; -.
DR BioCyc; ARA:AT3G25860-MON; -.
DR PRO; PR:Q9SQI8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SQI8; baseline and differential.
DR Genevisible; Q9SQI8; 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; IDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IDA:TAIR.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; TAS:TAIR.
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; 1.
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 PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Chloroplast; Glycolysis; Lipoyl; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..480
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component 4 of pyruvate dehydrogenase complex,
FT chloroplastic"
FT /id="PRO_0000430348"
FT DOMAIN 55..133
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 187..224
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 140..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 453
FT /evidence="ECO:0000255"
FT MOD_RES 96
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 480 AA; 50080 MW; 0D73F1990068300C CRC64;
MAVSSSSFLS TASLTNSKSN ISFASSVSPS LRSVVFRSTT PATSHRRSMT VRSKIREIFM
PALSSTMTEG KIVSWIKTEG EKLAKGESVV VVESDKADMD VETFYDGYLA AIVVGEGETA
PVGAAIGLLA ETEAEIEEAK SKAASKSSSS VAEAVVPSPP PVTSSPAPAI AQPAPVTAVS
DGPRKTVATP YAKKLAKQHK VDIESVAGTG PFGRITASDV ETAAGIAPSK SSIAPPPPPP
PPVTAKATTT NLPPLLPDSS IVPFTAMQSA VSKNMIESLS VPTFRVGYPV NTDALDALYE
KVKPKGVTMT ALLAKAAGMA LAQHPVVNAS CKDGKSFSYN SSINIAVAVA INGGLITPVL
QDADKLDLYL LSQKWKELVG KARSKQLQPH EYNSGTFTLS NLGMFGVDRF DAILPPGQGA
IMAVGASKPT VVADKDGFFS VKNTMLVNVT ADHRIVYGAD LAAFLQTFAK IIENPDSLTL
