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NAD(P)H-quinone oxidoreductase subunit T, chloroplastic (EC 1.6.5.-) (DNA J PROTEIN C75) (NAD(P)H dehydrogenase subunit T) (NDH subunit T) (NADH-plastoquinone oxidoreductase subunit T) (Protein CHLORORESPIRATORY REDUCTION J)

 NDHT_ARATH              Reviewed;         249 AA.
Q9SMS0; Q680H9;
04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-APR-2018, entry version 122.
RecName: Full=NAD(P)H-quinone oxidoreductase subunit T, chloroplastic {ECO:0000305};
EC=1.6.5.- {ECO:0000305};
AltName: Full=DNA J PROTEIN C75 {ECO:0000303|PubMed:23894646};
AltName: Full=NAD(P)H dehydrogenase subunit T {ECO:0000303|PubMed:21785130};
Short=NDH subunit T {ECO:0000305};
AltName: Full=NADH-plastoquinone oxidoreductase subunit T {ECO:0000305};
AltName: Full=Protein CHLORORESPIRATORY REDUCTION J {ECO:0000303|PubMed:21505067};
Flags: Precursor;
Name=ndhT {ECO:0000303|PubMed:21785130};
Synonyms=CRRJ {ECO:0000303|PubMed:21505067},
DJC75 {ECO:0000303|PubMed:23894646};
OrderedLocusNames=At4g09350 {ECO:0000312|Araport:AT4G09350};
ORFNames=T30A10.110 {ECO:0000312|EMBL:CAB55698.1};
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 [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).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-249.
STRAIN=cv. Columbia;
PubMed=14993207; DOI=10.1101/gr.1515604;
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G.,
Caboche M., Weissenbach J., Salanoubat M.;
"Whole genome sequence comparisons and 'full-length' cDNA sequences: a
combined approach to evaluate and improve Arabidopsis genome
annotation.";
Genome Res. 14:406-413(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-249.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
COMPONENT OF THE NDH COMPLEX, SUBUNIT, DISRUPTION PHENOTYPE,
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=21505067; DOI=10.1105/tpc.110.080291;
Yamamoto H., Peng L., Fukao Y., Shikanai T.;
"An Src homology 3 domain-like fold protein forms a ferredoxin binding
site for the chloroplast NADH dehydrogenase-like complex in
Arabidopsis.";
Plant Cell 23:1480-1493(2011).
[6]
NOMENCLATURE, AND COMPONENT OF THE NDH COMPLEX.
PubMed=21785130; DOI=10.1093/pcp/pcr098;
Ifuku K., Endo T., Shikanai T., Aro E.M.;
"Structure of the chloroplast NADH dehydrogenase-like complex:
nomenclature for nuclear-encoded subunits.";
Plant Cell Physiol. 52:1560-1568(2011).
[7]
COMPONENT OF THE NDH COMPLEX, AND SUBUNIT.
PubMed=24225949; DOI=10.1074/jbc.M113.511584;
Yamamoto H., Shikanai T.;
"In planta mutagenesis of Src homology 3 domain-like fold of NdhS, a
ferredoxin-binding subunit of the chloroplast NADH dehydrogenase-like
complex in Arabidopsis: a conserved Arg-193 plays a critical role in
ferredoxin binding.";
J. Biol. Chem. 288:36328-36337(2013).
[8]
IDENTIFICATION, NOMENCLATURE, AND SUBCELLULAR LOCATION.
PubMed=23894646; DOI=10.1371/journal.pone.0070384;
Chiu C.C., Chen L.J., Su P.H., Li H.M.;
"Evolution of chloroplast J proteins.";
PLoS ONE 8:E70384-E70384(2013).
-!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via
FMN and iron-sulfur (Fe-S) centers, to quinones in the
photosynthetic chain and possibly in a chloroplast respiratory
chain. The immediate electron acceptor for the enzyme in this
species is believed to be plastoquinone. Couples the redox
reaction to proton translocation, and thus conserves the redox
energy in a proton gradient (Probable). Required for the
accumulation of both the NDH subcomplex A and NDHS
(PubMed:21505067). {ECO:0000269|PubMed:21505067, ECO:0000305}.
-!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
plastoquinol. {ECO:0000305}.
-!- SUBUNIT: Part of the chloroplast NDH complex, composed of a
mixture of chloroplast and nucleus encoded subunits
(PubMed:21785130). Component of the electron donor-binding
subcomplex, at least composed of NDHS, NDHT and NDHU
(PubMed:21505067, PubMed:24225949). {ECO:0000269|PubMed:21505067,
ECO:0000269|PubMed:21785130, ECO:0000269|PubMed:24225949}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000269|PubMed:21505067, ECO:0000269|PubMed:23894646};
Single-pass membrane protein {ECO:0000255}.
-!- DISRUPTION PHENOTYPE: Malfunction of the NDH complex.
{ECO:0000269|PubMed:21505067}.
-----------------------------------------------------------------------
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EMBL; AL117386; CAB55698.1; -; Genomic_DNA.
EMBL; AL161514; CAB78058.1; -; Genomic_DNA.
EMBL; CP002687; AEE82744.1; -; Genomic_DNA.
EMBL; BX829231; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK175888; BAD43651.1; -; mRNA.
PIR; T17134; T17134.
RefSeq; NP_192673.1; NM_117003.3.
UniGene; At.33701; -.
ProteinModelPortal; Q9SMS0; -.
STRING; 3702.AT4G09350.1; -.
PaxDb; Q9SMS0; -.
DNASU; 826517; -.
EnsemblPlants; AT4G09350.1; AT4G09350.1; AT4G09350.
GeneID; 826517; -.
Gramene; AT4G09350.1; AT4G09350.1; AT4G09350.
KEGG; ath:AT4G09350; -.
Araport; AT4G09350; -.
TAIR; locus:2137961; AT4G09350.
eggNOG; KOG0715; Eukaryota.
eggNOG; COG0484; LUCA.
HOGENOM; HOG000243718; -.
OMA; VFFKEQY; -.
OrthoDB; EOG09360LE4; -.
PhylomeDB; Q9SMS0; -.
PRO; PR:Q9SMS0; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9SMS0; baseline and differential.
Genevisible; Q9SMS0; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IMP:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0010598; C:NAD(P)H dehydrogenase complex (plastoquinone); IMP:UniProtKB.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR036869; J_dom_sf.
Pfam; PF00226; DnaJ; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
Chaperone; Chloroplast; Complete proteome; Membrane; NAD; NADP;
Oxidoreductase; Plastid; Plastoquinone; Quinone; Reference proteome;
Thylakoid; Transit peptide; Transmembrane; Transmembrane helix;
Transport.
TRANSIT 1 45 Chloroplast. {ECO:0000305}.
CHAIN 46 249 NAD(P)H-quinone oxidoreductase subunit T,
chloroplastic.
/FTId=PRO_0000431816.
TRANSMEM 224 244 Helical. {ECO:0000255}.
DOMAIN 106 172 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
CONFLICT 154 154 E -> S (in Ref. 4; BAD43651).
{ECO:0000305}.
SEQUENCE 249 AA; 28496 MW; 9C71D29DD8C1466D CRC64;
MAYATSTYAR TSCIILPKIQ NGAHFTDDTK AFRRITARRV TRIYASQGPT KPSKPSPGVD
TRIHWESPDE GWIGGRSDPA KSVDEDKTNL LSDEKFAELI KDSFDSHYQF LGVSTDADLE
EIKSAYRRLS KEYHPDTTSL PLKTASEKFM KLREVYNVLS DEETRRFYDW TLAQEVASRQ
AEKMRMKLED PKEQDFRGYE SIPDMVDRLG GRNMELSDQA MTALTFDILI VLFAVCCIAF
VIVFKDPSY


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