ODP25_ARATH
ID ODP25_ARATH Reviewed; 465 AA.
AC Q9C8P0; Q8LGH6; Q9LNK4;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component 5 of pyruvate dehydrogenase complex, chloroplastic;
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide S-acetyltransferase component 5 of pyruvate dehydrogenase complex;
DE AltName: Full=Protein EMBRYO DEFECTIVE 3003;
DE AltName: Full=Pyruvate dehydrogenase complex component E2 5;
DE Short=PDC-E2 5;
DE Short=PDCE2 5;
DE Flags: Precursor;
GN Name=EMB3003; OrderedLocusNames=At1g34430; ORFNames=F12K21.24, F7P12.2;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79262.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC023279; AAF79262.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC023913; AAG51893.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31713.1; -; Genomic_DNA.
DR EMBL; AY128294; AAM91102.1; -; mRNA.
DR EMBL; BT001042; AAN46796.1; -; mRNA.
DR EMBL; AY084265; AAM60857.1; -; mRNA.
DR PIR; F86468; F86468.
DR RefSeq; NP_174703.1; NM_103166.4.
DR AlphaFoldDB; Q9C8P0; -.
DR SMR; Q9C8P0; -.
DR BioGRID; 25578; 15.
DR IntAct; Q9C8P0; 12.
DR STRING; 3702.AT1G34430.1; -.
DR MetOSite; Q9C8P0; -.
DR PaxDb; Q9C8P0; -.
DR PRIDE; Q9C8P0; -.
DR ProteomicsDB; 250877; -.
DR EnsemblPlants; AT1G34430.1; AT1G34430.1; AT1G34430.
DR GeneID; 840346; -.
DR Gramene; AT1G34430.1; AT1G34430.1; AT1G34430.
DR KEGG; ath:AT1G34430; -.
DR Araport; AT1G34430; -.
DR TAIR; locus:2009273; AT1G34430.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; Q9C8P0; -.
DR OMA; HSRVNKP; -.
DR OrthoDB; 747232at2759; -.
DR PhylomeDB; Q9C8P0; -.
DR BioCyc; ARA:AT1G34430-MON; -.
DR PRO; PR:Q9C8P0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8P0; baseline and differential.
DR Genevisible; Q9C8P0; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
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; 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..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 32..465
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component 5 of pyruvate dehydrogenase complex,
FT chloroplastic"
FT /id="PRO_0000430349"
FT DOMAIN 39..114
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 184..221
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 123..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /evidence="ECO:0000255"
FT MOD_RES 80
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 129..130
FT /note="Missing (in Ref. 4; AAM60857)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="P -> PP (in Ref. 4; AAM60857)"
FT /evidence="ECO:0000305"
FT CONFLICT 147..164
FT /note="AVEAPVSVEKKVAAAPVS -> TVVAPVAVEKKIAAPPVA (in Ref. 4;
FT AAM60857)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="K -> N (in Ref. 4; AAM60857)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="A -> V (in Ref. 4; AAM60857)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="G -> A (in Ref. 4; AAM60857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 48307 MW; F5B91FD25EC4B629 CRC64;
MSRLLQTPFL PSVSLPTKTR SSVTGFRVKP RIIPIQAKIR EIFMPALSST MTEGKIVSWV
KSEGDKLNKG ESVVVVESDK ADMDVETFYD GYLAAIMVEE GGVAPVGSAI ALLAETEDEI
ADAKAKASGG GGGGDSKAPP ASPPTAAVEA PVSVEKKVAA APVSIKAVAA SAVHPASEGG
KRIVASPYAK KLAKELKVEL AGLVGSGPMG RIVAKDVEAV AAGGGVQAAV AVKEVVAAPG
VELGSVVPFT TMQGAVSRNM VESLGVPTFR VGYTISTDAL DALYKKIKSK GVTMTALLAK
ATALALAKHP VVNSSCRDGN SFVYNSSINV AVAVAIDGGL ITPVLQNADK VDIYSLSRKW
KELVDKARAK QLQPQEYNTG TFTLSNLGMF GVDRFDAILP PGTGAIMAVG ASQPSVVATK
DGRIGMKNQM QVNVTADHRV IYGADLAQFL QTLASIIEDP KDLTF
