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Database: UniProt
Entry: NDHM_SYNPX
LinkDB: NDHM_SYNPX
Original site: NDHM_SYNPX 
ID   NDHM_SYNPX              Reviewed;         115 AA.
AC   Q7U417;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   07-NOV-2018, entry version 69.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit M {ECO:0000255|HAMAP-Rule:MF_01352};
DE            EC=1.6.5.- {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};
GN   OrderedLocusNames=SYNW2258;
OS   Synechococcus sp. (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L.,
RA   Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J.,
RA   Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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:0000255|HAMAP-Rule:MF_01352}.
CC   -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
CC       plastoquinol. {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
CC       identified which probably have different functions.
CC       {ECO:0000255|HAMAP-Rule:MF_01352}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01352}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01352}; Cytoplasmic side
CC       {ECO:0000255|HAMAP-Rule:MF_01352}.
CC   -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01352}.
DR   EMBL; BX569695; CAE08773.1; -; Genomic_DNA.
DR   RefSeq; WP_011129111.1; NC_005070.1.
DR   STRING; 84588.SYNW2258; -.
DR   EnsemblBacteria; CAE08773; CAE08773; SYNW2258.
DR   KEGG; syw:SYNW2258; -.
DR   eggNOG; ENOG4105GHY; Bacteria.
DR   eggNOG; ENOG4111NC5; LUCA.
DR   HOGENOM; HOG000069835; -.
DR   KO; K05584; -.
DR   OMA; PDNEFLW; -.
DR   OrthoDB; POG091H14SY; -.
DR   Proteomes; UP000001422; 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; Membrane; NAD; NADP; Oxidoreductase; Plastoquinone;
KW   Quinone; Reference proteome; Thylakoid; Transport.
FT   CHAIN         1    115       NAD(P)H-quinone oxidoreductase subunit M.
FT                                /FTId=PRO_0000352208.
SQ   SEQUENCE   115 AA;  12897 MW;  86E22A7DF75873F8 CRC64;
     MADTLLKCTT RHVRLFTARV DNQDLVPSAD ELTLDLDPDN EFLWSDAVVS KVQQRFQQLV
     EAGAGGELSD YSLRRIGTDL EGYIRQLLQA GELSYNPDGR VQNFSMGLPR TPDLL
//
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