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Database: UniProt
Entry: NDHM_ARATH
LinkDB: NDHM_ARATH
Original site: NDHM_ARATH 
ID   NDHM_ARATH              Reviewed;         217 AA.
AC   Q2V2S7; Q0WUL4; Q9SZJ4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   05-DEC-2018, entry version 79.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit M, chloroplastic {ECO:0000305};
DE            EC=1.6.5.- {ECO:0000305};
DE   AltName: Full=NAD(P)H dehydrogenase subunit M {ECO:0000303|PubMed:21785130};
DE            Short=NDH subunit M {ECO:0000305};
DE            Short=NDH-M {ECO:0000303|PubMed:15608332};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit M {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ndhM {ECO:0000303|PubMed:21785130};
GN   Synonyms=NDH-M {ECO:0000303|PubMed:15608332};
GN   OrderedLocusNames=At4g37925 {ECO:0000312|Araport:AT4G37925};
GN   ORFNames=F20D10.40 {ECO:0000312|EMBL:CAB37532.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA   Caboche M., Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome
RT   annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-217.
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.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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.,
RA   Peltier G.;
RT   "New subunits NDH-M, -N, and -O, encoded by nuclear genes, are
RT   essential for plastid Ndh complex functioning in higher plants.";
RL   Plant Cell 17:219-232(2005).
RN   [6]
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   [7]
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   [8]
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:
RT   nomenclature for nuclear-encoded subunits.";
RL   Plant Cell Physiol. 52:1560-1568(2011).
CC   -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via
CC       FMN and iron-sulfur (Fe-S) centers, to quinones in the
CC       photosynthetic chain and possibly in a chloroplast respiratory
CC       chain. The immediate electron acceptor for the enzyme in this
CC       species is believed to be plastoquinone. Couples the redox
CC       reaction to proton translocation, and thus conserves the redox
CC       energy in a proton gradient. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + H(+) + NADH = a plastoquinol + NAD(+);
CC         Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:62192; Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + H(+) + NADPH = a plastoquinol +
CC         NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561, Rhea:RHEA-
CC         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
CC       mixture of chloroplast and nucleus encoded subunits. Component of
CC       the NDH subcomplex A, at least composed of ndhH, ndhI, ndhJ, ndhK,
CC       ndhL, ndhM, 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 M family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB37532.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g37920 has been split into 2 genes: At4g37920 and At4g37925.; Evidence={ECO:0000305};
CC       Sequence=CAB80457.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g37920 has been split into 2 genes: At4g37920 and At4g37925.; Evidence={ECO:0000305};
DR   EMBL; AL035538; CAB37532.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161592; CAB80457.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86854.1; -; Genomic_DNA.
DR   EMBL; BX829112; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK227138; BAE99184.1; -; mRNA.
DR   PIR; T05619; T05619.
DR   RefSeq; NP_001031804.1; NM_001036727.3.
DR   UniGene; At.49770; -.
DR   BioGrid; 530952; 3.
DR   STRING; 3702.AT4G37925.1; -.
DR   TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   PaxDb; Q2V2S7; -.
DR   PRIDE; Q2V2S7; -.
DR   EnsemblPlants; AT4G37925.1; AT4G37925.1; AT4G37925.
DR   GeneID; 3770591; -.
DR   Gramene; AT4G37925.1; AT4G37925.1; AT4G37925.
DR   KEGG; ath:AT4G37925; -.
DR   Araport; AT4G37925; -.
DR   TAIR; locus:1009023311; AT4G37925.
DR   eggNOG; ENOG410IW88; Eukaryota.
DR   eggNOG; ENOG4111NC5; LUCA.
DR   HOGENOM; HOG000070913; -.
DR   OMA; MACTKFS; -.
DR   OrthoDB; EOG09360OLE; -.
DR   PhylomeDB; Q2V2S7; -.
DR   PRO; PR:Q2V2S7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q2V2S7; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; TAS:TAIR.
DR   GO; GO:0010598; C:NAD(P)H dehydrogenase complex (plastoquinone); TAS:TAIR.
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; IPR018922; NdhM.
DR   PANTHER; PTHR36900; PTHR36900; 1.
DR   Pfam; PF10664; NdhM; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Complete proteome; Membrane; NAD; NADP; Oxidoreductase;
KW   Plastid; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW   Transit peptide; Transport.
FT   TRANSIT       1     21       Chloroplast. {ECO:0000255}.
FT   CHAIN        22    217       NAD(P)H-quinone oxidoreductase subunit M,
FT                                chloroplastic.
FT                                /FTId=PRO_0000352661.
FT   CONFLICT     17     17       H -> D (in Ref. 4; BAE99184).
FT                                {ECO:0000305}.
SQ   SEQUENCE   217 AA;  24795 MW;  03E3DF014016BA2B CRC64;
     MVAAFSYTAC TKLSLLHPSM VAQIRPRTTQ KAFVVTNPEQ DSTLEVQETE TLKEEQSTEK
     MKKQPTPLRP VEKQLNVKSK GMGDFGGQWL SSVTRHVRIY AAYIDPETCE FDQSQMDKLT
     LILDPTEEFV WDDESCNKVY SYFQELVDHY EGAPLTEYTL RLIGSDVEHY IRKMLFDGEI
     QYNMDARVLN FSMGKPRVQF NTSNIEGGGD GQPQEDA
//
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