NDHO_ACAM1
ID NDHO_ACAM1 Reviewed; 69 AA.
AC B0BZU2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 67.
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=AM1_2137;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABW27152.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000828; ABW27152.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041660842.1; NC_009925.1.
DR AlphaFoldDB; B0BZU2; -.
DR SMR; B0BZU2; -.
DR STRING; 329726.AM1_2137; -.
DR EnsemblBacteria; ABW27152; ABW27152; AM1_2137.
DR KEGG; amr:AM1_2137; -.
DR eggNOG; ENOG5032XZT; Bacteria.
DR HOGENOM; CLU_195299_0_0_3; -.
DR OrthoDB; 1907204at2; -.
DR Proteomes; UP000000268; 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..69
FT /note="NAD(P)H-quinone oxidoreductase subunit O"
FT /id="PRO_0000353631"
SQ SEQUENCE 69 AA; 7773 MW; C49EF9CB397FF126 CRC64;
MAVKKGSLVR IVPEKFENSV EAKASDRRLP PYVFEGTGEV LEIKGDYAQI QFRVPVPTVW
LRVDQLEAA
