NDHO_THEVB
ID NDHO_THEVB Reviewed; 70 AA.
AC Q8DMU4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=tsl0017;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP PROTEIN SEQUENCE OF 16-44 AND 52-70, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15910282; DOI=10.1042/bj20050390;
RA Zhang P., Battchikova N., Paakkarinen V., Katoh H., Iwai M., Ikeuchi M.,
RA Pakrasi H.B., Ogawa T., Aro E.-M.;
RT "Isolation, subunit composition and interaction of the NDH-1 complexes from
RT Thermosynechococcus elongatus BP-1.";
RL Biochem. J. 390:513-520(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 {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I NdhO subunit family.
CC {ECO:0000305}.
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DR EMBL; BA000039; BAC07570.1; -; Genomic_DNA.
DR RefSeq; NP_680808.1; NC_004113.1.
DR RefSeq; WP_011055872.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; O=1-70.
DR PDB; 6KHI; EM; 3.00 A; O=1-70.
DR PDB; 6KHJ; EM; 3.00 A; O=1-70.
DR PDB; 6L7O; EM; 3.20 A; O=1-70.
DR PDB; 6L7P; EM; 3.60 A; O=1-70.
DR PDB; 6NBQ; EM; 3.10 A; O=1-70.
DR PDB; 6NBX; EM; 3.50 A; O=1-70.
DR PDB; 6NBY; EM; 3.10 A; O=1-70.
DR PDB; 6TJV; EM; 3.20 A; O=1-70.
DR PDBsum; 6HUM; -.
DR PDBsum; 6KHI; -.
DR PDBsum; 6KHJ; -.
DR PDBsum; 6L7O; -.
DR PDBsum; 6L7P; -.
DR PDBsum; 6NBQ; -.
DR PDBsum; 6NBX; -.
DR PDBsum; 6NBY; -.
DR PDBsum; 6TJV; -.
DR AlphaFoldDB; Q8DMU4; -.
DR SMR; Q8DMU4; -.
DR IntAct; Q8DMU4; 1.
DR STRING; 197221.22293738; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC07570; BAC07570; BAC07570.
DR KEGG; tel:tsl0017; -.
DR eggNOG; ENOG5032XZT; Bacteria.
DR OMA; TPNIWLR; -.
DR OrthoDB; 1907204at2; -.
DR Proteomes; UP000000440; 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 3D-structure; Direct protein sequencing; Membrane; NAD; NADP;
KW Plastoquinone; Quinone; Reference proteome; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..70
FT /note="NAD(P)H-quinone oxidoreductase subunit O"
FT /id="PRO_0000353651"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 38..51
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6KHI"
SQ SEQUENCE 70 AA; 7867 MW; DAFCC54E4A56DBDC CRC64;
MAIKKGDLVK VVAEKLANSL EALASDHRYP PYLFEGRGEV VDIRGDYAQI KFPVPTPTVW
LRLDQLEVAQ
