NDHO_SYNR3
ID NDHO_SYNR3 Reviewed; 74 AA.
AC A5GQL3;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=SynRCC307_0269;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
RG Genoscope;
RL Submitted (MAY-2006) 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}.
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; CT978603; CAK27172.1; -; Genomic_DNA.
DR RefSeq; WP_011934687.1; NC_009482.1.
DR AlphaFoldDB; A5GQL3; -.
DR SMR; A5GQL3; -.
DR STRING; 316278.SynRCC307_0269; -.
DR EnsemblBacteria; CAK27172; CAK27172; SynRCC307_0269.
DR KEGG; syr:SynRCC307_0269; -.
DR eggNOG; ENOG5032XZT; Bacteria.
DR HOGENOM; CLU_195299_0_0_3; -.
DR OMA; TPNIWLR; -.
DR OrthoDB; 1907204at2; -.
DR Proteomes; UP000001115; 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..74
FT /note="NAD(P)H-quinone oxidoreductase subunit O"
FT /id="PRO_0000353659"
SQ SEQUENCE 74 AA; 8065 MW; EA766D5396638EA0 CRC64;
MADALKKGSL IRVNREAYLS SVEAKASAGD PPAYLLEGPG EVLAVKGDYA QLRFRQPVPD
IWLRMDQLEA YAGS
