GenomeNet

Database: UniProt/SWISS-PROT
Entry: ODP24_ARATH
LinkDB: ODP24_ARATH
Original site: 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   16-JAN-2019, entry version 136.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   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-
RT   acetyltransferase subunit of the plastid pyruvate dehydrogenase
RT   complex (E2) from 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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   pyruvate dehydrogenase complex, in Arabidopsis causes an early embryo
RT   lethal 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
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA =
CC         (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:83100, 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=Translation N-terminally extended.; Evidence={ECO:0000305};
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   UniGene; At.23227; -.
DR   ProteinModelPortal; Q9SQI8; -.
DR   SMR; Q9SQI8; -.
DR   BioGrid; 7512; 10.
DR   IntAct; Q9SQI8; 4.
DR   STRING; 3702.AT3G25860.1; -.
DR   iPTMnet; Q9SQI8; -.
DR   SwissPalm; Q9SQI8; -.
DR   PaxDb; Q9SQI8; -.
DR   PRIDE; Q9SQI8; -.
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   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   InParanoid; Q9SQI8; -.
DR   KO; K00627; -.
DR   OMA; HEIDINK; -.
DR   OrthoDB; 747232at2759; -.
DR   PhylomeDB; Q9SQI8; -.
DR   BioCyc; ARA:AT3G25860-MONOMER; -.
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; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
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; IPR036625; E3-bd_dom_sf.
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   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Chloroplast; Complete proteome; Glycolysis; Lipoyl;
KW   Plastid; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT       1     47       Chloroplast. {ECO:0000255}.
FT   CHAIN        48    480       Dihydrolipoyllysine-residue
FT                                acetyltransferase component 4 of pyruvate
FT                                dehydrogenase complex, chloroplastic.
FT                                /FTId=PRO_0000430348.
FT   DOMAIN       55    133       Lipoyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN      187    224       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01170}.
FT   COMPBIAS    235    242       Poly-Pro.
FT   ACT_SITE    453    453       {ECO:0000255}.
FT   MOD_RES      96     96       N6-lipoyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-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
//
DBGET integrated database retrieval system