ID   NDHO_SYNSC              Reviewed;          84 AA.
AC   Q3AH38;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Syncc9605_2362;
OS   Synechococcus sp. (strain CC9605).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=110662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9605;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9605.";
RL   Submitted (JUL-2005) 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; CP000110; ABB36094.1; -; Genomic_DNA.
DR   RefSeq; WP_006850906.1; NC_007516.1.
DR   AlphaFoldDB; Q3AH38; -.
DR   SMR; Q3AH38; -.
DR   STRING; 110662.Syncc9605_2362; -.
DR   EnsemblBacteria; ABB36094; ABB36094; Syncc9605_2362.
DR   KEGG; syd:Syncc9605_2362; -.
DR   eggNOG; ENOG5032XZT; Bacteria.
DR   HOGENOM; CLU_195299_0_0_3; -.
DR   OMA; TPNIWLR; -.
DR   OrthoDB; 1907204at2; -.
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; Thylakoid; Translocase;
KW   Transport.
FT   CHAIN           1..84
FT                   /note="NAD(P)H-quinone oxidoreductase subunit O"
FT                   /id="PRO_0000353655"
SQ   SEQUENCE   84 AA;  8946 MW;  E6A57708F4C49C2C CRC64;
     MAESDAAAPA KAKPAALRKG ALVKVNRAAY SSSLEAGASD PTAPDYIFEG PGELLVVKGD
     YGQVRWNRPV PDVWLRMDQL EACS