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NDHO_ARATH
ID   NDHO_ARATH              Reviewed;         158 AA.
AC   Q9S829;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit O, chloroplastic {ECO:0000305};
DE            EC=7.1.1.- {ECO:0000305};
DE   AltName: Full=NAD(P)H dehydrogenase subunit O {ECO:0000303|PubMed:21785130};
DE            Short=NDH subunit O {ECO:0000305};
DE            Short=NDH-O {ECO:0000303|PubMed:15608332};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit O {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ndhO {ECO:0000303|PubMed:21785130};
GN   Synonyms=NDH-O {ECO:0000303|PubMed:15608332};
GN   OrderedLocusNames=At1g74880 {ECO:0000312|Araport:AT1G74880};
GN   ORFNames=F25A4.15 {ECO:0000312|EMBL:AAD55288.1},
GN   F9E10.27 {ECO:0000312|EMBL:AAG51918.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   COMPONENT OF THE NDH COMPLEX, AND DISRUPTION PHENOTYPE.
RX   PubMed=15608332; DOI=10.1105/tpc.104.028282;
RA   Rumeau D., Becuwe-Linka N., Beyly A., Louwagie M., Garin J., Peltier G.;
RT   "New subunits NDH-M, -N, and -O, encoded by nuclear genes, are essential
RT   for plastid Ndh complex functioning in higher plants.";
RL   Plant Cell 17:219-232(2005).
RN   [5]
RP   REVIEW.
RX   PubMed=19995722; DOI=10.1093/mp/ssp052;
RA   Suorsa M., Sirpioe S., Aro E.M.;
RT   "Towards characterization of the chloroplast NAD(P)H dehydrogenase
RT   complex.";
RL   Mol. Plant 2:1127-1140(2009).
RN   [6]
RP   REVIEW.
RX   PubMed=21029720; DOI=10.1016/j.bbabio.2010.10.015;
RA   Peng L., Yamamoto H., Shikanai T.;
RT   "Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase
RT   complex.";
RL   Biochim. Biophys. Acta 1807:945-953(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).
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. {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. Component of the NDH
CC       subcomplex A, at least composed of ndhH, ndhI, ndhJ, ndhK, ndhL, ndhM,
CC       ndhN and ndhO. {ECO:0000269|PubMed:15608332,
CC       ECO:0000269|PubMed:21785130}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250|UniProtKB:Q9CAC5}; Peripheral membrane protein
CC       {ECO:0000305}; Stromal side {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Malfunction of the NDH complex.
CC       {ECO:0000269|PubMed:15608332}.
CC   -!- SIMILARITY: Belongs to the NDH complex subunit O family. {ECO:0000305}.
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DR   EMBL; AC008263; AAD55288.1; -; Genomic_DNA.
DR   EMBL; AC013258; AAG51918.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35643.1; -; Genomic_DNA.
DR   EMBL; AF344320; AAK06871.1; -; mRNA.
DR   EMBL; AF410289; AAK95275.1; -; mRNA.
DR   EMBL; AY143808; AAN28747.1; -; mRNA.
DR   PIR; D96778; D96778.
DR   RefSeq; NP_565093.1; NM_106146.5.
DR   AlphaFoldDB; Q9S829; -.
DR   SMR; Q9S829; -.
DR   STRING; 3702.AT1G74880.1; -.
DR   TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   MetOSite; Q9S829; -.
DR   PaxDb; Q9S829; -.
DR   PRIDE; Q9S829; -.
DR   ProteomicsDB; 251127; -.
DR   EnsemblPlants; AT1G74880.1; AT1G74880.1; AT1G74880.
DR   GeneID; 843827; -.
DR   Gramene; AT1G74880.1; AT1G74880.1; AT1G74880.
DR   KEGG; ath:AT1G74880; -.
DR   Araport; AT1G74880; -.
DR   TAIR; locus:2027247; AT1G74880.
DR   eggNOG; ENOG502RZEJ; Eukaryota.
DR   HOGENOM; CLU_130659_0_0_1; -.
DR   InParanoid; Q9S829; -.
DR   OMA; QFTVKAE; -.
DR   OrthoDB; 1498012at2759; -.
DR   PhylomeDB; Q9S829; -.
DR   PRO; PR:Q9S829; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9S829; baseline and differential.
DR   Genevisible; Q9S829; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0010598; C:NAD(P)H dehydrogenase complex (plastoquinone); TAS:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0010258; P:NADH dehydrogenase complex (plastoquinone) assembly; IMP:TAIR.
DR   InterPro; IPR020905; NdhO.
DR   Pfam; PF11910; NdhO; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Reference proteome; Thylakoid; Transit peptide; Translocase; Transport.
FT   TRANSIT         1..38
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..158
FT                   /note="NAD(P)H-quinone oxidoreductase subunit O,
FT                   chloroplastic"
FT                   /id="PRO_0000431815"
FT   REGION          33..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   158 AA;  17657 MW;  0E314C448A040EA1 CRC64;
     MAFSATVSQL SSLSTISSSL PISSRRLPHR SLPQFTVKAE AEKEKQSTQG KSDGEASPAA
     TKTPKTLPKK PVYSMKKGQI VRVEKEKYLN SINYLSVGHP PFYKGLDYIY EDRGEVLDLR
     VFETGEYALV GWVGIPTAPA WLPTDMLIKC EKLVYERM
 
 
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