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Dihydrolipoyl dehydrogenase 1, chloroplastic (ptLPD1) (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase 1) (Protein LIPOAMIDE DEHYDROGENASE 1) (Pyruvate dehydrogenase complex E3 subunit 1) (E3-1) (PDC-E3 1)

 PLPD1_ARATH             Reviewed;         623 AA.
A8MS68; B9DG34; Q9M5K5;
18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 1.
25-OCT-2017, entry version 80.
RecName: Full=Dihydrolipoyl dehydrogenase 1, chloroplastic;
Short=ptLPD1;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase 1;
AltName: Full=Protein LIPOAMIDE DEHYDROGENASE 1;
AltName: Full=Pyruvate dehydrogenase complex E3 subunit 1;
Short=E3-1;
Short=PDC-E3 1;
Flags: Precursor;
Name=LPD1; OrderedLocusNames=At3g16950; ORFNames=K14A17.6;
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] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, 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=10819329; DOI=10.1093/dnares/7.2.131;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
features of the regions of 4,504,864 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:131-135(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[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:0000269|PubMed:11056213}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=A8MS68-1; Sequence=Displayed;
Name=2;
IsoId=A8MS68-2; Sequence=VSP_047927, VSP_047928;
-!- 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; AF228637; AAF37698.1; -; mRNA.
EMBL; AB026636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002686; AEE75887.1; -; Genomic_DNA.
EMBL; CP002686; AEE75888.1; -; Genomic_DNA.
EMBL; AY050376; AAK91394.1; -; mRNA.
EMBL; AY120695; AAM52238.1; -; mRNA.
EMBL; AK317007; BAH19701.1; -; mRNA.
RefSeq; NP_001078165.1; NM_001084696.1. [A8MS68-1]
RefSeq; NP_566562.1; NM_112571.3. [A8MS68-2]
UniGene; At.16905; -.
ProteinModelPortal; A8MS68; -.
SMR; A8MS68; -.
BioGrid; 6284; 2.
IntAct; A8MS68; 1.
STRING; 3702.AT3G16950.2; -.
PaxDb; A8MS68; -.
PRIDE; A8MS68; -.
EnsemblPlants; AT3G16950.1; AT3G16950.1; AT3G16950. [A8MS68-2]
EnsemblPlants; AT3G16950.2; AT3G16950.2; AT3G16950. [A8MS68-1]
GeneID; 820951; -.
Gramene; AT3G16950.1; AT3G16950.1; AT3G16950.
Gramene; AT3G16950.2; AT3G16950.2; AT3G16950.
KEGG; ath:AT3G16950; -.
Araport; AT3G16950; -.
TAIR; locus:2086177; AT3G16950.
eggNOG; KOG1335; Eukaryota.
eggNOG; COG1249; LUCA.
HOGENOM; HOG000276708; -.
KO; K00382; -.
OMA; GTCINWG; -.
OrthoDB; EOG093607YW; -.
PhylomeDB; A8MS68; -.
PRO; PR:A8MS68; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; A8MS68; baseline and differential.
Genevisible; A8MS68; 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:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; ISS:TAIR.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; TAS:TAIR.
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.
InterPro; IPR006258; Lipoamide_DH.
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.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
2: Evidence at transcript level;
Alternative splicing; Chloroplast; Complete proteome; Disulfide bond;
FAD; Flavoprotein; NAD; Oxidoreductase; Plastid; Redox-active center;
Reference proteome; Transit peptide.
TRANSIT 1 70 Chloroplast. {ECO:0000255}.
CHAIN 71 623 Dihydrolipoyl dehydrogenase 1,
chloroplastic.
/FTId=PRO_0000423493.
NP_BIND 116 124 FAD. {ECO:0000250}.
NP_BIND 224 226 FAD. {ECO:0000250}.
NP_BIND 261 268 NAD. {ECO:0000250}.
NP_BIND 409 412 FAD. {ECO:0000250}.
ACT_SITE 539 539 Proton acceptor. {ECO:0000250}.
BINDING 133 133 FAD. {ECO:0000250}.
BINDING 199 199 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 284 284 NAD. {ECO:0000250}.
BINDING 357 357 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 403 403 FAD. {ECO:0000250}.
DISULFID 124 129 Redox-active. {ECO:0000250}.
VAR_SEQ 564 570 GDAKIKL -> VSEKVVV (in isoform 2).
{ECO:0000303|PubMed:11056213,
ECO:0000303|PubMed:14593172}.
/FTId=VSP_047927.
VAR_SEQ 571 623 Missing (in isoform 2).
{ECO:0000303|PubMed:11056213,
ECO:0000303|PubMed:14593172}.
/FTId=VSP_047928.
CONFLICT 14 14 F -> L (in Ref. 5; BAH19701).
{ECO:0000305}.
CONFLICT 222 222 I -> T (in Ref. 5; BAH19701).
{ECO:0000305}.
SEQUENCE 623 AA; 66661 MW; 6747C79E1D2DE365 CRC64;
MQSAMALSFS QTSFTRPNHV LGSSGSVFST PRSLRFCGLR REAFGFSTSN QLAIRSNRIQ
FLSRKSFQVS ASASSNGNGA PPKSFDYDLI IIGAGVGGHG AALHAVEKGL KTAIIEGDVV
GGTCVNRGCV PSKALLAVSG RMRELQNEHH MKSFGLQVSA AGYDRQGVAD HANNLATKIR
NNLTNSMKAI GVDILTGFGS VLGPQKVKYG KDNIITAKDI IIATGSVPFV PKGIEVDGKT
VITSDHALKL ESVPEWIAIV GSGYIGLEFS DVYTALGSEV TFIEALDQLM PGFDPEISKL
AQRVLINPRK IDYHTGVFAS KITPARDGKP VLIELIDAKT KEPKDTLEVD AALIATGRAP
FTNGLGLENV NVVTQRGFIP VDERMRVIDG KGTLVPNLYC IGDANGKLML AHAASAQGIS
VVEQVSGRDH VLNHLSIPAA CFTHPEISMV GLTEPQAKEK GEKEGFKVSV VKTSFKANTK
ALAENEGEGI AKMIYRPDNG EILGVHIFGL HAADLIHEAS NAIALGTRIQ DIKLAVHAHP
TLSEVLDELF KAAKVESHAT TRTGDAKIKL NTNQEDRKGR RRGGDDEKQP SVSKDLKDIS
TRPSSFFENI SVGVLSLLSL IFV


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