ID   NDHO_RIPO1              Reviewed;          72 AA.
AC   B7JVP1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
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            Short=NDH-1 subunit O {ECO:0000255|HAMAP-Rule:MF_01354};
DE            Short=NDH-O {ECO:0000255|HAMAP-Rule:MF_01354};
GN   Name=ndhO {ECO:0000255|HAMAP-Rule:MF_01354};
GN   OrderedLocusNames=PCC8801_0521;
OS   Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX   NCBI_TaxID=41431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001287; ACK64612.1; -; Genomic_DNA.
DR   RefSeq; WP_012593889.1; NC_011726.1.
DR   AlphaFoldDB; B7JVP1; -.
DR   SMR; B7JVP1; -.
DR   STRING; 41431.PCC8801_0521; -.
DR   EnsemblBacteria; ACK64612; ACK64612; PCC8801_0521.
DR   KEGG; cyp:PCC8801_0521; -.
DR   eggNOG; ENOG5032XZT; Bacteria.
DR   HOGENOM; CLU_195299_0_0_3; -.
DR   OMA; TPNIWLR; -.
DR   OrthoDB; 1907204at2; -.
DR   Proteomes; UP000008204; 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..72
FT                   /note="NAD(P)H-quinone oxidoreductase subunit O"
FT                   /id="PRO_1000143677"
SQ   SEQUENCE   72 AA;  8166 MW;  E11DE3F6FA17D5FC CRC64;
     MAAKMKKGAL VRAVKETLEN SLEAQASDSR FPSYLFDSKG EILDLTDEYA LVRFYVPTPS
     VWLRLDQLEL AE