ID   NDHM_PROM0              Reviewed;         115 AA.
AC   A3PAL2;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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}; OrderedLocusNames=P9301_01641;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000576; ABO16787.1; -; Genomic_DNA.
DR   RefSeq; WP_011862190.1; NC_009091.1.
DR   AlphaFoldDB; A3PAL2; -.
DR   SMR; A3PAL2; -.
DR   STRING; 167546.P9301_01641; -.
DR   EnsemblBacteria; ABO16787; ABO16787; P9301_01641.
DR   KEGG; pmg:P9301_01641; -.
DR   eggNOG; ENOG5031AQM; Bacteria.
DR   HOGENOM; CLU_137431_0_0_3; -.
DR   OMA; PDNEFLW; -.
DR   Proteomes; UP000001430; 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_0000352189"
SQ   SEQUENCE   115 AA;  13420 MW;  0E867B40ED7B93FA CRC64;
     MEKMLLKSTT RHVRIFTAEV VDEELKFHPN KLTLDLDPDN EFIWNEDSLN KINEKFNGLI
     KERAGKDLDD YELRKIGSEI EGLIKFLLQN GQLSYNPDCR VMNYSMGLPM TNEVL