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Dihydrolipoyl dehydrogenase 2, chloroplastic (ptLPD2) (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase 2) (Protein LIPOAMIDE DEHYDROGENASE 2) (Pyruvate dehydrogenase complex E3 subunit 2) (E3-2) (PDC-E3 2)

 PLPD2_ARATH             Reviewed;         567 AA.
F4JLP5; Q9M5K4;
18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
18-SEP-2013, sequence version 2.
22-NOV-2017, entry version 54.
RecName: Full=Dihydrolipoyl dehydrogenase 2, chloroplastic;
Short=ptLPD2;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase 2;
AltName: Full=Protein LIPOAMIDE DEHYDROGENASE 2;
AltName: Full=Pyruvate dehydrogenase complex E3 subunit 2;
Short=E3-2;
Short=PDC-E3 2;
Flags: Precursor;
Name=LPD2; OrderedLocusNames=At4g16155; ORFNames=FCAALL.61;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11056213; DOI=10.1016/S0014-5793(00)02116-5;
Lutziger I., Oliver D.J.;
"Molecular evidence of a unique lipoamide dehydrogenase in plastids:
analysis of plastidic lipoamide dehydrogenase from Arabidopsis
thaliana.";
FEBS Lett. 484:12-16(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9461215; DOI=10.1038/35140;
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L.,
Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
Arabidopsis thaliana.";
Nature 391:485-488(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
DISRUPTION PHENOTYPE.
PubMed=20488895; DOI=10.1104/pp.110.153452;
Chen W., Chi Y., Taylor N.L., Lambers H., Finnegan P.M.;
"Disruption of ptLPD1 or ptLPD2, genes that encode isoforms of the
plastidial lipoamide dehydrogenase, confers arsenate hypersensitivity
in Arabidopsis.";
Plant Physiol. 153:1385-1397(2010).
-!- FUNCTION: Lipoamide dehydrogenase is a component of the plastidial
pyruvate dehydrogenase complex (PDC).
{ECO:0000269|PubMed:11056213}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer (By similarity). Part of the plastidial
pyruvate dehydrogenase complex (PDC) containing multiple copies of
three enzymatic components: pyruvate dehydrogenase (E1),
dihydrolipoamide acetyltransferase (E2) and lipoamide
dehydrogenase (E3). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed mainly in flower buds and immature
siliques, and to a lesser extent in flowers.
{ECO:0000269|PubMed:11056213}.
-!- DISRUPTION PHENOTYPE: Arsenate hypersensitivity.
{ECO:0000269|PubMed:20488895}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF228638; AAF37699.1; -; mRNA.
EMBL; Z97340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL161543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002687; AEE83704.2; -; Genomic_DNA.
EMBL; AY050877; AAK92814.1; -; mRNA.
EMBL; AY054195; AAL06856.1; -; mRNA.
EMBL; AY113958; AAM45006.1; -; mRNA.
RefSeq; NP_567487.5; NM_117711.8.
UniGene; At.16906; -.
UniGene; At.20170; -.
ProteinModelPortal; F4JLP5; -.
SMR; F4JLP5; -.
BioGrid; 12601; 1.
STRING; 3702.AT4G16155.1; -.
PaxDb; F4JLP5; -.
PRIDE; F4JLP5; -.
EnsemblPlants; AT4G16155.1; AT4G16155.1; AT4G16155.
GeneID; 827307; -.
Gramene; AT4G16155.1; AT4G16155.1; AT4G16155.
KEGG; ath:AT4G16155; -.
Araport; AT4G16155; -.
TAIR; locus:505006477; AT4G16155.
eggNOG; KOG1335; Eukaryota.
eggNOG; COG1249; LUCA.
HOGENOM; HOG000276708; -.
InParanoid; F4JLP5; -.
KO; K00382; -.
OrthoDB; EOG093607YW; -.
PhylomeDB; F4JLP5; -.
PRO; PR:F4JLP5; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; F4JLP5; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0046685; P:response to arsenic-containing substance; IMP:UniProtKB.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
2: Evidence at transcript level;
Chloroplast; Complete proteome; Disulfide bond; FAD; Flavoprotein;
NAD; Oxidoreductase; Plastid; Redox-active center; Reference proteome;
Transit peptide.
TRANSIT 1 67 Chloroplast. {ECO:0000255}.
CHAIN 68 567 Dihydrolipoyl dehydrogenase 2,
chloroplastic.
/FTId=PRO_0000423494.
NP_BIND 114 122 FAD. {ECO:0000250}.
NP_BIND 221 223 FAD. {ECO:0000250}.
NP_BIND 258 265 NAD. {ECO:0000250}.
NP_BIND 406 409 FAD. {ECO:0000250}.
ACT_SITE 536 536 Proton acceptor. {ECO:0000250}.
BINDING 131 131 FAD. {ECO:0000250}.
BINDING 197 197 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 281 281 NAD. {ECO:0000250}.
BINDING 354 354 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 400 400 FAD. {ECO:0000250}.
DISULFID 122 127 Redox-active. {ECO:0000250}.
SEQUENCE 567 AA; 60145 MW; BAC2D3EE9BB4D250 CRC64;
MQSVLSLSFS QASLPLANRT LCSSNAAPST PRNLRFCGLR REAFCFSPSK QLTSCRFHIQ
SRRIEVSAAA SSSAGNGAPS KSFDYDLIII GAGVGGHGAA LHAVEKGLKT AIIEGDVVGG
TCVNRGCVPS KALLAVSGRM RELQNEHHMK AFGLQVSAAG YDRQGVADHA SNLATKIRNN
LTNSMKALGV DILTGFGAVL GPQKVKYGDN IITGKDIIIA TGSVPFVPKG IEVDGKTVIT
SDHALKLESV PDWIAIVGSG YIGLEFSDVY TALGSEVTFI EALDQLMPGF DPEISKLAQR
VLINTRKIDY HTGVFASKIT PAKDGKPVLI ELIDAKTKEP KDTLEVDAAL IATGRAPFTN
GLGLENINVT TQRGFIPVDE RMRVIDGNGK LVPHLYCIGD ANGKLMLAHA ASAQGISVVE
QVTGRDHVLN HLSIPAACFT HPEISMVGLT EPQAREKAEK EGFKVSIAKT SFKANTKALA
ENEGEGLAKM IYRPDNGEIL GVHIFGLHAA DLIHEASNAI ALGTRIQDIK LAVHAHPTLS
EVVDELFKAA KVDSPASVTA QSVKVTV


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