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 03-AUG-2022, entry version 92.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit M, chloroplastic {ECO:0000305};
DE EC=7.1.1.- {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; 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].
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 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., Hayashizaki Y.,
RA 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., 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 [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: 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 M family. {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};
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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 PDB; 7WFG; EM; 4.33 A; M=1-217.
DR PDB; 7WG5; EM; 3.89 A; M=1-217.
DR PDBsum; 7WFG; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q2V2S7; -.
DR SMR; Q2V2S7; -.
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 ProteomicsDB; 251321; -.
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; ENOG502QUN1; Eukaryota.
DR HOGENOM; CLU_089187_0_0_1; -.
DR OMA; GQMEDVN; -.
DR OrthoDB; 1404408at2759; -.
DR PhylomeDB; Q2V2S7; -.
DR PRO; PR:Q2V2S7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q2V2S7; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA: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:0005886; C:plasma membrane; HDA: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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone;
KW Quinone; Reference proteome; Thylakoid; Transit peptide; Translocase;
KW Transport.
FT TRANSIT 1..21
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 22..217
FT /note="NAD(P)H-quinone oxidoreductase subunit M,
FT chloroplastic"
FT /id="PRO_0000352661"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 17
FT /note="H -> D (in Ref. 4; BAE99184)"
FT /evidence="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
