ID   NDHM_SYNS9              Reviewed;         115 AA.
AC   Q3B058;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit M {ECO:0000255|HAMAP-Rule:MF_01352};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01352};
DE   AltName: Full=NAD(P)H dehydrogenase I subunit M {ECO:0000255|HAMAP-Rule:MF_01352};
DE            Short=NDH-1 subunit M {ECO:0000255|HAMAP-Rule:MF_01352};
DE            Short=NDH-M {ECO:0000255|HAMAP-Rule:MF_01352};
GN   Name=ndhM {ECO:0000255|HAMAP-Rule:MF_01352};
GN   OrderedLocusNames=Syncc9902_0297;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC       FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC       and/or the photosynthetic chain. The immediate electron acceptor for
CC       the enzyme in this species is believed to be plastoquinone. Couples the
CC       redox reaction to proton translocation, and thus conserves the redox
CC       energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC       inorganic carbon-concentration. {ECO:0000255|HAMAP-Rule:MF_01352}.
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:0000255|HAMAP-Rule:MF_01352};
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:0000255|HAMAP-Rule:MF_01352};
CC   -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC       different subcomplexes with different compositions have been identified
CC       which probably have different functions. {ECO:0000255|HAMAP-
CC       Rule:MF_01352}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01352}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01352}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01352}.
CC   -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01352}.
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DR   EMBL; CP000097; ABB25270.1; -; Genomic_DNA.
DR   RefSeq; WP_011359128.1; NC_007513.1.
DR   AlphaFoldDB; Q3B058; -.
DR   SMR; Q3B058; -.
DR   STRING; 316279.Syncc9902_0297; -.
DR   EnsemblBacteria; ABB25270; ABB25270; Syncc9902_0297.
DR   KEGG; sye:Syncc9902_0297; -.
DR   eggNOG; ENOG5031AQM; Bacteria.
DR   HOGENOM; CLU_137431_0_0_3; -.
DR   OMA; PDNEFLW; -.
DR   OrthoDB; 1815256at2; -.
DR   Proteomes; UP000002712; Chromosome.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01352; NDH1_NDH1M; 1.
DR   InterPro; IPR018922; NdhM.
DR   PANTHER; PTHR36900; PTHR36900; 1.
DR   Pfam; PF10664; NdhM; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW   Translocase; Transport.
FT   CHAIN           1..115
FT                   /note="NAD(P)H-quinone oxidoreductase subunit M"
FT                   /id="PRO_0000352203"
SQ   SEQUENCE   115 AA;  13057 MW;  216A864715EDE35F CRC64;
     MADTLLKCTT RHVRLFTARV DNDDLVPSAN ELTLDLDPDN EFIWSESCIS QVQQRFKQLV
     DAAAGGELSD YTLRRIGTDL EGFIRQLLQR GELSYNPEAR VQNFSMGLPR TPELL