ID   NDHO_SYNY3              Reviewed;          72 AA.
AC   P74771;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit O;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase I subunit O;
DE   AltName: Full=NDH-1 subunit O;
DE   AltName: Full=NDH-O;
GN   Name=ndhO; OrderedLocusNames=ssl1690;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 16-64, CHARACTERIZATION AS A MEMBER OF THE
RP   NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX   PubMed=15548534; DOI=10.1074/jbc.m410914200;
RA   Battchikova N., Zhang P., Rudd S., Ogawa T., Aro E.-M.;
RT   "Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes
RT   of Synechocystis sp. PCC 6803.";
RL   J. Biol. Chem. 280:2587-2595(2005).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16287171; DOI=10.1002/pmic.200500111;
RA   Srivastava R., Pisareva T., Norling B.;
RT   "Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC
RT   6803.";
RL   Proteomics 5:4905-4916(2005).
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 (By similarity). {ECO:0000250}.
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   -!- 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   -!- 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.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000305|PubMed:16287171}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:16287171}; Cytoplasmic side
CC       {ECO:0000305|PubMed:16287171}.
CC   -!- SIMILARITY: Belongs to the complex I NdhO subunit family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000022; BAA10471.1; -; Genomic_DNA.
DR   PIR; S75736; S75736.
DR   AlphaFoldDB; P74771; -.
DR   SMR; P74771; -.
DR   IntAct; P74771; 1.
DR   STRING; 1148.1673312; -.
DR   PaxDb; P74771; -.
DR   EnsemblBacteria; BAA10471; BAA10471; BAA10471.
DR   KEGG; syn:ssl1690; -.
DR   eggNOG; ENOG5032XZT; Bacteria.
DR   InParanoid; P74771; -.
DR   OMA; TPNIWLR; -.
DR   Proteomes; UP000001425; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW   Reference proteome; Thylakoid; Translocase; Transport.
FT   CHAIN           1..72
FT                   /note="NAD(P)H-quinone oxidoreductase subunit O"
FT                   /id="PRO_0000353662"
SQ   SEQUENCE   72 AA;  8289 MW;  57B91A6F10B29610 CRC64;
     MAAKMKKGSL VRVIRAQLEN SLEAQASDRR LPDYLFHSKG EVLDLNEEYA LVRFYVPTPN
     VWLRLDQIEA LA