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Database: UniProt/SWISS-PROT
Entry: ODP25_ARATH
LinkDB: ODP25_ARATH
Original site: 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   16-JAN-2019, entry version 129.
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;
GN   ORFNames=F12K21.24, F7P12.2;
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 [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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
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   [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
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 {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};
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   UniGene; At.15055; -.
DR   UniGene; At.72010; -.
DR   ProteinModelPortal; Q9C8P0; -.
DR   SMR; Q9C8P0; -.
DR   BioGrid; 25578; 10.
DR   IntAct; Q9C8P0; 12.
DR   STRING; 3702.AT1G34430.1; -.
DR   PaxDb; Q9C8P0; -.
DR   PRIDE; Q9C8P0; -.
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   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   InParanoid; Q9C8P0; -.
DR   KO; K00627; -.
DR   OMA; RCRVEAK; -.
DR   OrthoDB; 747232at2759; -.
DR   PhylomeDB; Q9C8P0; -.
DR   BioCyc; ARA:AT1G34430-MONOMER; -.
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; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
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     31       Chloroplast. {ECO:0000255}.
FT   CHAIN        32    465       Dihydrolipoyllysine-residue
FT                                acetyltransferase component 5 of pyruvate
FT                                dehydrogenase complex, chloroplastic.
FT                                /FTId=PRO_0000430349.
FT   DOMAIN       39    114       Lipoyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN      184    221       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01170}.
FT   ACT_SITE    438    438       {ECO:0000255}.
FT   MOD_RES      80     80       N6-lipoyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   CONFLICT    129    130       Missing (in Ref. 4; AAM60857).
FT                                {ECO:0000305}.
FT   CONFLICT    139    139       P -> PP (in Ref. 4; AAM60857).
FT                                {ECO:0000305}.
FT   CONFLICT    147    164       AVEAPVSVEKKVAAAPVS -> TVVAPVAVEKKIAAPPVA
FT                                (in Ref. 4; AAM60857). {ECO:0000305}.
FT   CONFLICT    197    197       K -> N (in Ref. 4; AAM60857).
FT                                {ECO:0000305}.
FT   CONFLICT    238    238       A -> V (in Ref. 4; AAM60857).
FT                                {ECO:0000305}.
FT   CONFLICT    265    265       G -> A (in Ref. 4; AAM60857).
FT                                {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
//
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