NDHO_NOSP7
ID NDHO_NOSP7 Reviewed; 71 AA.
AC B2J5F9;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, 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}; OrderedLocusNames=Npun_R3935;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) 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; CP001037; ACC82316.1; -; Genomic_DNA.
DR RefSeq; WP_012410284.1; NC_010628.1.
DR AlphaFoldDB; B2J5F9; -.
DR SMR; B2J5F9; -.
DR STRING; 63737.Npun_R3935; -.
DR EnsemblBacteria; ACC82316; ACC82316; Npun_R3935.
DR KEGG; npu:Npun_R3935; -.
DR eggNOG; ENOG5032XZT; Bacteria.
DR HOGENOM; CLU_195299_0_0_3; -.
DR OMA; TPNIWLR; -.
DR OrthoDB; 1907204at2; -.
DR PhylomeDB; B2J5F9; -.
DR Proteomes; UP000001191; 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..71
FT /note="NAD(P)H-quinone oxidoreductase subunit O"
FT /id="PRO_0000353637"
SQ SEQUENCE 71 AA; 8143 MW; AF6F4AFB32128B7A CRC64;
MAVKKGDMVR AIREKLENSL EAKASDTRFP PYLFDSKGEI VDIKGDYALI KFGKVPTPNV
WLRVDQLEEF K