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Database: UniProt
Entry: A5GJP1
LinkDB: A5GJP1
Original site: A5GJP1 
ID   NDHL_SYNPW              Reviewed;          81 AA.
AC   A5GJP1;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   01-MAY-2013, entry version 33.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit L;
DE            EC=1.6.5.-;
DE   AltName: Full=NAD(P)H dehydrogenase I subunit L;
DE   AltName: Full=NDH-1 subunit L;
DE   AltName: Full=NDH-L;
GN   Name=ndhL; OrderedLocusNames=SynWH7803_0730;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) 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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
CC       plastoquinol.
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 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NdhL subunit family.
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DR   EMBL; CT971583; CAK23156.1; -; Genomic_DNA.
DR   RefSeq; YP_001224453.1; NC_009481.1.
DR   STRING; 32051.SynWH7803_0730; -.
DR   EnsemblBacteria; CAK23156; CAK23156; SynWH7803_0730.
DR   GeneID; 5146548; -.
DR   KEGG; syx:SynWH7803_0730; -.
DR   PATRIC; 23827569; VBISynSp43824_0749.
DR   eggNOG; NOG08765; -.
DR   HOGENOM; HOG000022604; -.
DR   KO; K05583; -.
DR   OMA; MNNRWNV; -.
DR   ProtClustDB; CLSK893123; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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:HAMAP.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01355; NDH1_NDH1L; 1; -.
DR   InterPro; IPR019654; NADH-quinone_OxRdatse_su_L.
DR   Pfam; PF10716; NdhL; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Membrane; NAD; NADP; Oxidoreductase; Plastoquinone;
KW   Quinone; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1     81       NAD(P)H-quinone oxidoreductase subunit L.
FT                                /FTId=PRO_0000353693.
FT   TRANSMEM     13     33       Helical; (Potential).
FT   TRANSMEM     51     71       Helical; (Potential).
SQ   SEQUENCE   81 AA;  9142 MW;  6E2E45EED2DDB033 CRC64;
     METLLNAIPQ ETLLVIGAYG ALGAAYLVVI PLFLYFWMNR RWTVMGKLER LGIYGLVFLF
     FPGLILFAPF LNLRMSGQGD V
//
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