NDHT_ARATH
ID NDHT_ARATH Reviewed; 249 AA.
AC Q9SMS0; Q680H9;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit T, chloroplastic {ECO:0000305};
DE EC=7.1.1.- {ECO:0000305};
DE AltName: Full=DNA J PROTEIN C75 {ECO:0000303|PubMed:23894646};
DE AltName: Full=NAD(P)H dehydrogenase subunit T {ECO:0000303|PubMed:21785130};
DE Short=NDH subunit T {ECO:0000305};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit T {ECO:0000305};
DE AltName: Full=Protein CHLORORESPIRATORY REDUCTION J {ECO:0000303|PubMed:21505067};
DE Flags: Precursor;
GN Name=ndhT {ECO:0000303|PubMed:21785130};
GN Synonyms=CRRJ {ECO:0000303|PubMed:21505067},
GN DJC75 {ECO:0000303|PubMed:23894646};
GN OrderedLocusNames=At4g09350 {ECO:0000312|Araport:AT4G09350};
GN ORFNames=T30A10.110 {ECO:0000312|EMBL:CAB55698.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] OF 2-249.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-249.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP COMPONENT OF THE NDH COMPLEX, SUBUNIT, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=21505067; DOI=10.1105/tpc.110.080291;
RA Yamamoto H., Peng L., Fukao Y., Shikanai T.;
RT "An Src homology 3 domain-like fold protein forms a ferredoxin binding site
RT for the chloroplast NADH dehydrogenase-like complex in Arabidopsis.";
RL Plant Cell 23:1480-1493(2011).
RN [6]
RP NOMENCLATURE, AND COMPONENT OF THE NDH COMPLEX.
RX PubMed=21785130; DOI=10.1093/pcp/pcr098;
RA Ifuku K., Endo T., Shikanai T., Aro E.M.;
RT "Structure of the chloroplast NADH dehydrogenase-like complex: nomenclature
RT for nuclear-encoded subunits.";
RL Plant Cell Physiol. 52:1560-1568(2011).
RN [7]
RP COMPONENT OF THE NDH COMPLEX, AND SUBUNIT.
RX PubMed=24225949; DOI=10.1074/jbc.m113.511584;
RA Yamamoto H., Shikanai T.;
RT "In planta mutagenesis of Src homology 3 domain-like fold of NdhS, a
RT ferredoxin-binding subunit of the chloroplast NADH dehydrogenase-like
RT complex in Arabidopsis: a conserved Arg-193 plays a critical role in
RT ferredoxin binding.";
RL J. Biol. Chem. 288:36328-36337(2013).
RN [8]
RP IDENTIFICATION, NOMENCLATURE, AND SUBCELLULAR LOCATION.
RX PubMed=23894646; DOI=10.1371/journal.pone.0070384;
RA Chiu C.C., Chen L.J., Su P.H., Li H.M.;
RT "Evolution of chloroplast J proteins.";
RL PLoS ONE 8:E70384-E70384(2013).
CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC and possibly in a chloroplast respiratory chain. The immediate electron
CC acceptor for the enzyme in this species is believed to be
CC plastoquinone. Couples the redox reaction to proton translocation, and
CC thus conserves the redox energy in a proton gradient (Probable).
CC Required for the accumulation of both the NDH subcomplex A and NDHS
CC (PubMed:21505067). {ECO:0000269|PubMed:21505067, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Part of the chloroplast NDH complex, composed of a mixture of
CC chloroplast and nucleus encoded subunits (PubMed:21785130). Component
CC of the electron donor-binding subcomplex, at least composed of NDHS,
CC NDHT and NDHU (PubMed:21505067, PubMed:24225949).
CC {ECO:0000269|PubMed:21505067, ECO:0000269|PubMed:21785130,
CC ECO:0000269|PubMed:24225949}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:21505067, ECO:0000269|PubMed:23894646}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Malfunction of the NDH complex.
CC {ECO:0000269|PubMed:21505067}.
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DR EMBL; AL117386; CAB55698.1; -; Genomic_DNA.
DR EMBL; AL161514; CAB78058.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82744.1; -; Genomic_DNA.
DR EMBL; BX829231; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK175888; BAD43651.1; -; mRNA.
DR PIR; T17134; T17134.
DR RefSeq; NP_192673.1; NM_117003.3.
DR AlphaFoldDB; Q9SMS0; -.
DR SMR; Q9SMS0; -.
DR STRING; 3702.AT4G09350.1; -.
DR PaxDb; Q9SMS0; -.
DR PRIDE; Q9SMS0; -.
DR ProteomicsDB; 251128; -.
DR DNASU; 826517; -.
DR EnsemblPlants; AT4G09350.1; AT4G09350.1; AT4G09350.
DR GeneID; 826517; -.
DR Gramene; AT4G09350.1; AT4G09350.1; AT4G09350.
DR KEGG; ath:AT4G09350; -.
DR Araport; AT4G09350; -.
DR TAIR; locus:2137961; AT4G09350.
DR eggNOG; KOG0715; Eukaryota.
DR HOGENOM; CLU_081125_0_0_1; -.
DR InParanoid; Q9SMS0; -.
DR OMA; CCIIYAV; -.
DR OrthoDB; 1378665at2759; -.
DR PhylomeDB; Q9SMS0; -.
DR PRO; PR:Q9SMS0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SMS0; baseline and differential.
DR Genevisible; Q9SMS0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010598; C:NAD(P)H dehydrogenase complex (plastoquinone); IMP:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR044618; NdhT-like.
DR PANTHER; PTHR45283; PTHR45283; 1.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone;
KW Quinone; Reference proteome; Thylakoid; Transit peptide; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 46..249
FT /note="NAD(P)H-quinone oxidoreductase subunit T,
FT chloroplastic"
FT /id="PRO_0000431816"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 106..172
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 44..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 154
FT /note="E -> S (in Ref. 4; BAD43651)"
FT /evidence="ECO:0000305"
SQ 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
