NDHS_ARATH
ID NDHS_ARATH Reviewed; 250 AA.
AC Q9T0A4; Q93Z46;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit S, chloroplastic {ECO:0000305};
DE EC=7.1.1.- {ECO:0000305};
DE AltName: Full=NAD(P)H dehydrogenase subunit S {ECO:0000303|PubMed:21785130};
DE Short=NDH subunit S {ECO:0000305};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit S {ECO:0000305};
DE AltName: Full=Protein CHLORORESPIRATORY REDUCTION 31 {ECO:0000303|PubMed:21505067};
DE Flags: Precursor;
GN Name=ndhS {ECO:0000303|PubMed:21785130};
GN Synonyms=CRR31 {ECO:0000303|PubMed:21505067};
GN OrderedLocusNames=At4g23890 {ECO:0000312|Araport:AT4G23890};
GN ORFNames=T32A16.60 {ECO:0000312|EMBL:CAB43889.1};
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 {ECO:0000312|Proteomes:UP000006548};
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].
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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA 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].
RC STRAIN=cv. Columbia;
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.
RN [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-52, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
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 [7]
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 [8]
RP COMPONENT OF THE NDH COMPLEX, SUBUNIT, MUTAGENESIS OF ARG-193, AND
RP FUNCTION.
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).
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 efficient operation of ferredoxin-dependent
CC plastoquinone reduction. Forms the electron donor-binding subcomplex in
CC association with the NDHT and NDHU subunits (PubMed:21505067,
CC PubMed:24225949). {ECO:0000269|PubMed:21505067,
CC ECO:0000269|PubMed:24225949, 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. Interacts with the NDH subcomplex A via the protein NDHT
CC 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}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21505067}; Stromal side
CC {ECO:0000269|PubMed:21505067}.
CC -!- PTM: Arg-193 is the critical site for the high affinity binding of NDH
CC to ferredoxin.
CC -!- DISRUPTION PHENOTYPE: Malfunction of the NDH complex.
CC {ECO:0000269|PubMed:21505067}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25559.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL078468; CAB43889.1; -; Genomic_DNA.
DR EMBL; AL161560; CAB81307.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84820.1; -; Genomic_DNA.
DR EMBL; AY058143; AAL25559.1; ALT_FRAME; mRNA.
DR EMBL; AY128349; AAM91552.1; -; mRNA.
DR EMBL; BT000002; AAN15321.1; -; mRNA.
DR EMBL; AY087028; AAM64589.1; -; mRNA.
DR PIR; T08908; T08908.
DR RefSeq; NP_194120.1; NM_118521.3.
DR AlphaFoldDB; Q9T0A4; -.
DR SMR; Q9T0A4; -.
DR STRING; 3702.AT4G23890.1; -.
DR iPTMnet; Q9T0A4; -.
DR PaxDb; Q9T0A4; -.
DR PRIDE; Q9T0A4; -.
DR ProteomicsDB; 251167; -.
DR EnsemblPlants; AT4G23890.1; AT4G23890.1; AT4G23890.
DR GeneID; 828489; -.
DR Gramene; AT4G23890.1; AT4G23890.1; AT4G23890.
DR KEGG; ath:AT4G23890; -.
DR Araport; AT4G23890; -.
DR TAIR; locus:2138091; AT4G23890.
DR eggNOG; ENOG502RXJM; Eukaryota.
DR HOGENOM; CLU_094759_0_0_1; -.
DR InParanoid; Q9T0A4; -.
DR OMA; CAKFDLF; -.
DR OrthoDB; 1481220at2759; -.
DR PhylomeDB; Q9T0A4; -.
DR PRO; PR:Q9T0A4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0A4; baseline and differential.
DR Genevisible; Q9T0A4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IMP:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010598; C:NAD(P)H dehydrogenase complex (plastoquinone); IMP:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IMP:UniProtKB.
DR InterPro; IPR021659; NdhS.
DR PANTHER; PTHR35494; PTHR35494; 1.
DR Pfam; PF11623; NdhS; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isopeptide bond; Membrane; NAD; NADP; Plastid; Plastoquinone;
KW Quinone; Reference proteome; Thylakoid; Transit peptide; Translocase;
KW Transport; Ubl conjugation.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..250
FT /note="NAD(P)H-quinone oxidoreductase subunit S,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431818"
FT REGION 76..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT MUTAGEN 193
FT /note="R->Q,A,E,D: Strongly decreases the NDH ferredoxin-
FT dependent plastoquinone reduction."
SQ SEQUENCE 250 AA; 27727 MW; 71525402A5D8C32D CRC64;
MATSSITIPT IRTPIHRSKF LGQTHQFSTV NRSVFPPPKQ QSKLYQVKAM GKFNLWEVMG
GRGLCNGEKG IEKELQRNIE DEQETSKAEN NETERESDDS NLSFKVPEDG FEKEMMGLTG
GFPGGEKGLK TFIEKNPPPP PPPPPAKQGS DASAVATDKK PKAPKLPLLM PGMIAIVKNQ
NSPYHMYCGI VQRITDGKAG VLFEGGNWDR LITFRLEELE RREKGPPGKN PKSCILEPLI
EQMQKEEAAP
