Database: UniProt
Entry: A0A077JL60_9CYAN
LinkDB: A0A077JL60_9CYAN
Original site: A0A077JL60_9CYAN 
ID   A0A077JL60_9CYAN        Unreviewed;       118 AA.
AC   A0A077JL60;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   23-MAY-2018, entry version 15.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE            EC=1.6.5.- {ECO:0000256|HAMAP-Rule:MF_01352};
DE   AltName: Full=NAD(P)H dehydrogenase I subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE            Short=NDH-1 subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE            Short=NDH-M {ECO:0000256|HAMAP-Rule:MF_01352};
GN   Name=ndhO {ECO:0000313|EMBL:BAP18313.1};
GN   Synonyms=ndhM {ECO:0000256|HAMAP-Rule:MF_01352};
GN   ORFNames=ETSB_1588 {ECO:0000313|EMBL:BAP18313.1};
OS   cyanobacterium endosymbiont of Epithemia turgida isolate EtSB Lake
OS   Yunoko.
OC   Bacteria; Cyanobacteria.
OX   NCBI_TaxID=1228987 {ECO:0000313|EMBL:BAP18313.1};
RN   [1] {ECO:0000313|EMBL:BAP18313.1}
RC   STRAIN=ETSB Lake Yunoko {ECO:0000313|EMBL:BAP18313.1};
RX   PubMed=25049384; DOI=10.1073/pnas.1405222111;
RA   Nakayama T., Kamikawa R., Tanifuji G., Kashiyama Y., Ohkouchi N.,
RA   Archibald J.M., Inagaki Y.;
RT   "Complete genome of a nonphotosynthetic cyanobacterium in a diatom
RT   reveals recent adaptations to an intracellular lifestyle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11407-11412(2014).
CC   -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor,
CC       via FMN and iron-sulfur (Fe-S) centers, to quinones in the
CC       respiratory and/or the photosynthetic chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       plastoquinone. Couples the redox reaction to proton translocation,
CC       and thus conserves the redox energy in a proton gradient.
CC       Cyanobacterial NDH-1 also plays a role in inorganic carbon-
CC       concentration. {ECO:0000256|HAMAP-Rule:MF_01352}.
CC   -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
CC       plastoquinol. {ECO:0000256|HAMAP-Rule:MF_01352}.
CC   -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC       different subcomplexes with different compositions have been
CC       identified which probably have different functions.
CC       {ECO:0000256|HAMAP-Rule:MF_01352}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01352}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01352}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_01352}.
CC   -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01352}.
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DR   EMBL; AP012549; BAP18313.1; -; Genomic_DNA.
DR   RefSeq; WP_044107142.1; NZ_AP012549.1.
DR   EnsemblBacteria; BAP18313; BAP18313; ETSB_1588.
DR   KEGG; ceo:ETSB_1588; -.
DR   KO; K05584; -.
DR   GO; GO:0042651; C: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 {ECO:0000256|HAMAP-Rule:MF_01352};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01352};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01352}.
SQ   SEQUENCE   118 AA;  13629 MW;  08C3D7F967963F4A CRC64;
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