Database: UniProt
Entry: K9PXZ6_9CYAN
Original site: K9PXZ6_9CYAN 
ID   K9PXZ6_9CYAN            Unreviewed;       120 AA.
AC   K9PXZ6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   28-FEB-2018, entry version 24.
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=ndhM {ECO:0000256|HAMAP-Rule:MF_01352};
GN   ORFNames=Lepto7376_1664 {ECO:0000313|EMBL:AFY37998.1};
OS   Leptolyngbya sp. PCC 7376.
OC   Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=111781 {ECO:0000313|EMBL:AFY37998.1, ECO:0000313|Proteomes:UP000010389};
RN   [1] {ECO:0000313|EMBL:AFY37998.1, ECO:0000313|Proteomes:UP000010389}
RC   STRAIN=PCC 7376 {ECO:0000313|Proteomes:UP000010389};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA   Woyke T., Kerfeld C.;
RT   "Finished genome of Leptolyngbya sp. PCC 7376.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003946; AFY37998.1; -; Genomic_DNA.
DR   RefSeq; WP_015133768.1; NC_019683.1.
DR   EnsemblBacteria; AFY37998; AFY37998; Lepto7376_1664.
DR   KEGG; lep:Lepto7376_1664; -.
DR   PATRIC; fig|111781.3.peg.1895; -.
DR   KO; K05584; -.
DR   OrthoDB; POG091H14SY; -.
DR   BioCyc; LSP111781:G1HCI-1657-MONOMER; -.
DR   Proteomes; UP000010389; Chromosome.
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   Complete proteome {ECO:0000313|Proteomes:UP000010389};
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   Reference proteome {ECO:0000313|Proteomes:UP000010389};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01352}.
SQ   SEQUENCE   120 AA;  14046 MW;  5DA374B4AD6EBB4B CRC64;
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