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Database: UniProt
Entry: A0A0C2QF95_9CYAN
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ID   A0A0C2QF95_9CYAN        Unreviewed;       124 AA.
AC   A0A0C2QF95;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   31-JAN-2018, entry version 14.
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=SD80_19605 {ECO:0000313|EMBL:KIJ82514.1};
OS   Scytonema tolypothrichoides VB-61278.
OC   Bacteria; Cyanobacteria; Nostocales; Scytonemataceae; Scytonema.
OX   NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ82514.1, ECO:0000313|Proteomes:UP000031959};
RN   [1] {ECO:0000313|EMBL:KIJ82514.1, ECO:0000313|Proteomes:UP000031959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ82514.1,
RC   ECO:0000313|Proteomes:UP000031959};
RA   Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.;
RT   "Draft genome sequence of Scytonema tolypothrichoides VB-61278.";
RL   Submitted (JAN-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KIJ82514.1}.
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DR   EMBL; JXCA01000011; KIJ82514.1; -; Genomic_DNA.
DR   RefSeq; WP_048869884.1; NZ_JXCA01000011.1.
DR   EnsemblBacteria; KIJ82514; KIJ82514; SD80_19605.
DR   Proteomes; UP000031959; Unassembled WGS sequence.
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:UP000031959};
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:UP000031959};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01352}.
SQ   SEQUENCE   124 AA;  13993 MW;  6800412D787DBEBA CRC64;
     MDNPMLLKST TRHIRIFAGE IDQDGELVPS SQVLTLDVDP DNEFNWNEDA LQKVYRKFDE
     LVEASSGADL IDYNLRRIGS DLEHFLRSLL QKGEVSYNLS ARVTNYSMGL PQVASEENTE
     SNGV
//
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