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Database: UniProt
Entry: A0A0K2LYM3_9NOST
LinkDB: A0A0K2LYM3_9NOST
Original site: A0A0K2LYM3_9NOST 
ID   A0A0K2LYM3_9NOST        Unreviewed;       118 AA.
AC   A0A0K2LYM3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   31-JAN-2018, entry version 12.
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=AA650_10980 {ECO:0000313|EMBL:ALB40930.1};
OS   Anabaena sp. WA102.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB40930.1, ECO:0000313|Proteomes:UP000056652};
RN   [1] {ECO:0000313|EMBL:ALB40930.1, ECO:0000313|Proteomes:UP000056652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA102 {ECO:0000313|EMBL:ALB40930.1,
RC   ECO:0000313|Proteomes:UP000056652};
RA   Brown N.M.;
RT   "The finished genome of an anatoxin-a-producing Anabaena isolate
RT   reveals extensive genome rearrangement.";
RL   Submitted (MAY-2015) 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; CP011456; ALB40930.1; -; Genomic_DNA.
DR   RefSeq; WP_027400788.1; NZ_CP011456.1.
DR   EnsemblBacteria; ALB40930; ALB40930; AA650_10980.
DR   KEGG; awa:AA650_10980; -.
DR   PATRIC; fig|1647413.5.peg.2578; -.
DR   KO; K05584; -.
DR   Proteomes; UP000056652; 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:UP000056652};
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;  13597 MW;  16EFEF20C221E8CA CRC64;
     MDNLILLKST TRHVRIFAAE MDKDELIPSN QVLTLDIDPD NEFNWNEDAL QKVYRQFDQL
     VEASSGEDLT DYNLRRIGSD LEHYLRSLLQ KGEISYNLSS RVTNYSMGLP QVVTSSNQ
//
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