NDHO_SYNS9
ID NDHO_SYNS9 Reviewed; 84 AA.
AC Q3B027;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Syncc9902_0328;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-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; CP000097; ABB25300.1; -; Genomic_DNA.
DR RefSeq; WP_011359157.1; NC_007513.1.
DR AlphaFoldDB; Q3B027; -.
DR SMR; Q3B027; -.
DR STRING; 316279.Syncc9902_0328; -.
DR EnsemblBacteria; ABB25300; ABB25300; Syncc9902_0328.
DR KEGG; sye:Syncc9902_0328; -.
DR eggNOG; ENOG5032XZT; Bacteria.
DR HOGENOM; CLU_195299_0_0_3; -.
DR OMA; TPNIWLR; -.
DR OrthoDB; 1907204at2; -.
DR Proteomes; UP000002712; 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..84
FT /note="NAD(P)H-quinone oxidoreductase subunit O"
FT /id="PRO_0000353656"
SQ SEQUENCE 84 AA; 9133 MW; F7C08300782FEB8F CRC64;
MADSDTSAPA KAKPAALRKG ALVKVNRKAY SASIEAAASD PTPPDYIFDG PGELLVVKGD
YGQVRWNRPV PDVWLRMDQL EVYS