AC MF_01358; DC Protein; auto TR HAMAP; MF_01358; -; 1; level=0 XX Names: NDH1_NuoD XX case ID NDHH DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, chloroplastic; DE EC=7.1.1.-; DE AltName: Full=NAD(P)H dehydrogenase, subunit H; DE AltName: Full=NADH-plastoquinone oxidoreductase 49 kDa subunit; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H; GN Name=ndhH; else case ID NDHH DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H; DE EC=7.1.1.-; DE AltName: Full=NAD(P)H dehydrogenase, subunit H; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H; DE AltName: Full=NDH-1 subunit H; DE Short=NDH-H; GN Name=ndhH; else ID NUOD DE RecName: Full=NADH-quinone oxidoreductase subunit D; DE EC=7.1.1.-; DE AltName: Full=NADH dehydrogenase I subunit D; DE AltName: Full=NDH-1 subunit D; GN Name=nuoD; end case XX case CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain CC and possibly in a chloroplast respiratory chain. The immediate electron CC acceptor for the enzyme in this species is believed to be CC plastoquinone. Couples the redox reaction to proton translocation, and CC thus conserves the redox energy in a proton gradient. else case 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. else case or or or or CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. The immediate CC electron acceptor for the enzyme in this species is believed to be a CC menaquinone. Couples the redox reaction to proton translocation (for CC every two electrons transferred, four hydrogen ions are translocated CC across the cytoplasmic membrane), and thus conserves the redox energy CC in a proton gradient. else CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. The immediate CC electron acceptor for the enzyme in this species is believed to be CC ubiquinone. Couples the redox reaction to proton translocation (for CC every two electrons transferred, four hydrogen ions are translocated CC across the cytoplasmic membrane), and thus conserves the redox energy CC in a proton gradient. end case case or 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; else CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; end case case CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. else case 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. else case CC -!- SUBUNIT: NDH-1 is composed of 15 different subunits. Subunits NuoB, C, CC D, E, F, and G constitute the peripheral sector of the complex. else CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C, CC D, E, F, and G constitute the peripheral sector of the complex. end case case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; CC Peripheral membrane protein; Stromal side. else case and not CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane CC protein; Cytoplasmic side. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; CC Cytoplasmic side. else case not defined or CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; CC Cytoplasmic side. end case CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. XX DR PROSITE; PS00535; COMPLEX1_49K; 1; trigger=no DR Pfam; PF00346; Complex1_49kDa; 1; trigger=no DR NCBIfam; TIGR01962; NuoD; 1; trigger=no XX KW NAD case or KW NADP KW Plastoquinone else case not and not and not and not and not KW Ubiquinone end case KW Quinone KW Membrane KW Translocase KW Transport case or and not KW Thylakoid else case KW Cell membrane KW Cell inner membrane else case not defined or KW Cell membrane else case KW Cell membrane KW Cell inner membrane end case XX case or GO GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor GO GO:0019684; P:photosynthesis, light reaction else GO GO:0050136; F:NADH dehydrogenase (quinone) activity end case case and not GO GO:0042651; C:thylakoid membrane else case GO GO:0009535; C:chloroplast thylakoid membrane else GO GO:0005886; C:plasma membrane end case XX Size: 364-482; Related: MF_01359!; MF_01397!; Template: P33599; P27724; Scope: Bacteria Plastid Fusion: Nter: None Cter: None Duplicate: in KORVE, ANADE, ANADF, ANASK, BEII9, CHLAA, CHLT3, CYTH3, GLOVI, HERA2, NITHX, OPITP, RHIE6, RHIEC, RHIME, ROSCS, ROSS1, SALAI, SALTO, SINMW, SOLUE, SORC5, STRAW, STRCO, STRGG, STRM5, SYMTH, THEYD Plasmid: in BEII9, RHIME, SINMW Comments: 14 proteins form the NDH-1 complex in most bacteria, there are at least 15 subunits in cyanobacteria and chloroplasts. PARDE and THET8 are annotated with another nomenclature. In some bacteria this protein is fused with nuoD, see families MF_01359 and MF_01397. In many bacteria there are both the individual and fused versions. XX # Revision 1.25 2023/06/15 //