ID   NDHO_PROMP              Reviewed;          80 AA.
AC   Q7V3F4;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 86.
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}; OrderedLocusNames=PMM0121;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548174; CAE18580.1; -; Genomic_DNA.
DR   RefSeq; WP_011131760.1; NC_005072.1.
DR   AlphaFoldDB; Q7V3F4; -.
DR   SMR; Q7V3F4; -.
DR   STRING; 59919.PMM0121; -.
DR   EnsemblBacteria; CAE18580; CAE18580; PMM0121.
DR   KEGG; pmm:PMM0121; -.
DR   eggNOG; ENOG5031XXZ; Bacteria.
DR   HOGENOM; CLU_195299_0_0_3; -.
DR   OrthoDB; 1907204at2; -.
DR   Proteomes; UP000001026; 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; Thylakoid; Translocase;
KW   Transport.
FT   CHAIN           1..80
FT                   /note="NAD(P)H-quinone oxidoreductase subunit O"
FT                   /id="PRO_0000353649"
SQ   SEQUENCE   80 AA;  9219 MW;  19A642863632D7CA CRC64;
     MTESIPKKPL KKGSLVFIDK SIYDGSVEAL ASDQDLPSYI FEGPGEILSI KEEYAQVRWR
     RPVPDVWFKL DQIKEYIVSE