ID   NDHO_PAUCH              Reviewed;          82 AA.
AC   B1X470;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit O, organellar chromatophore {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}; OrderedLocusNames=PCC_0297;
OS   Paulinella chromatophora.
OG   Plastid; Organellar chromatophore.
OC   Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC   Paulinellidae; Paulinella.
OX   NCBI_TaxID=39717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA   Nowack E.C.M., Melkonian M., Gloeckner G.;
RT   "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT   photosynthesis by eukaryotes.";
RL   Curr. Biol. 18:410-418(2008).
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: Plastid, organellar chromatophore thylakoid
CC       membrane {ECO:0000250}; 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; CP000815; ACB42739.1; -; Genomic_DNA.
DR   RefSeq; YP_002048949.1; NC_011087.1.
DR   AlphaFoldDB; B1X470; -.
DR   SMR; B1X470; -.
DR   GeneID; 6481371; -.
DR   GO; GO:0070118; C:organellar chromatophore thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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; Organellar chromatophore; Plastid; Plastoquinone;
KW   Quinone; Thylakoid; Translocase.
FT   CHAIN           1..82
FT                   /note="NAD(P)H-quinone oxidoreductase subunit O, organellar
FT                   chromatophore"
FT                   /id="PRO_0000353664"
SQ   SEQUENCE   82 AA;  9074 MW;  7315AAE9C99FBC46 CRC64;
     MNEFQTESFV SLKPYDLVKV NRGAYVGSLE ARASDPIPPA YIFEGPGTLI TTAGQYSLVR
     WHLIPAPDVW LATAQLEAYS ED