ID   NDHO_SYNP2              Reviewed;          71 AA.
AC   B1XI93;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit O {ECO:0000255|HAMAP-Rule:MF_01354};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01354};
DE   AltName: Full=NAD(P)H dehydrogenase I subunit O {ECO:0000255|HAMAP-Rule:MF_01354};
DE   AltName: Full=NDH-1 subunit O;
DE   AltName: Full=NDH-O;
GN   Name=ndhO {ECO:0000255|HAMAP-Rule:MF_01354};
GN   OrderedLocusNames=SYNPCC7002_A2094;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC       FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC       and/or the photosynthetic chain. The immediate electron acceptor for
CC       the enzyme in this species is believed to be plastoquinone. Couples the
CC       redox reaction to proton translocation, and thus conserves the redox
CC       energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC       inorganic carbon-concentration. {ECO:0000255|HAMAP-Rule:MF_01354}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01354};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC         H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01354};
CC   -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC       different subcomplexes with different compositions have been identified
CC       which probably have different functions. {ECO:0000255|HAMAP-
CC       Rule:MF_01354}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01354}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01354}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01354}.
CC   -!- SIMILARITY: Belongs to the complex I NdhO subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01354}.
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DR   EMBL; CP000951; ACB00078.1; -; Genomic_DNA.
DR   RefSeq; WP_012307699.1; NC_010475.1.
DR   AlphaFoldDB; B1XI93; -.
DR   SMR; B1XI93; -.
DR   STRING; 32049.SYNPCC7002_A2094; -.
DR   EnsemblBacteria; ACB00078; ACB00078; SYNPCC7002_A2094.
DR   KEGG; syp:SYNPCC7002_A2094; -.
DR   eggNOG; ENOG5032XZT; Bacteria.
DR   HOGENOM; CLU_195299_0_0_3; -.
DR   OMA; TPNIWLR; -.
DR   Proteomes; UP000001688; Chromosome.
DR   GO; GO:0031676; C:plasma membrane-derived 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_01354; NDH1_NDH1O; 1.
DR   InterPro; IPR020905; NdhO.
DR   Pfam; PF11910; NdhO; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW   Translocase; Transport.
FT   CHAIN           1..71
FT                   /note="NAD(P)H-quinone oxidoreductase subunit O"
FT                   /id="PRO_0000353653"
SQ   SEQUENCE   71 AA;  8072 MW;  8391F8B389C91C6E CRC64;
     MAAKLKKGSL VRVIKEQFTN SLEAKASDSR LPAYFFGSQG EILDLDDEYA FVRFYTPTPS
     VWLRLDQLEA V