AC MF_01350; DC Protein; auto TR HAMAP; MF_01350; -; 1; level=0 XX Names: NDH1_NuoH XX case ID NU1C DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic; DE EC=7.1.1.-; DE AltName: Full=NAD(P)H dehydrogenase subunit 1; DE Short=NDH subunit 1; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 1; GN Name=ndhA; else case ID NU1C DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1; DE EC=7.1.1.-; DE AltName: Full=NAD(P)H dehydrogenase I subunit 1; DE AltName: Full=NDH-1 subunit 1; DE AltName: Full=NDH-A; GN Name=ndhA; else case ID FPOH DE RecName: Full=F(420)H(2) dehydrogenase subunit H; DE EC=1.5.98.3; DE AltName: Full=F(420)H(2)-dependent phenazine dehydrogenase subunit H; DE AltName: Full=F(420)H(2)-dependent phenazine oxidoreductase subunit H; DE Short=FPO subunit H; GN Name=fpoH; else ID NUOH DE RecName: Full=NADH-quinone oxidoreductase subunit H; DE EC=7.1.1.-; DE AltName: Full=NADH dehydrogenase I subunit H; DE AltName: Full=NDH-1 subunit H; GN Name=nuoH; 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. else case CC -!- FUNCTION: Component of the F(420)H(2) dehydrogenase (FPO complex) which CC is part of the energy-conserving F(420)H(2):heterodisulfide CC oxidoreductase system. The membrane-bound electron transfer system of CC the complex plays an important role in the metabolism of methylotrophic CC methanogens when the organisms grow on methanol or methylamines. CC Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. CC It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) CC centers, to methanophenazine (an electron carrier in the membrane). It CC couples the redox reaction to proton translocation (for every two CC electrons transferred, two hydrogen ions are translocated across the CC cytoplasmic membrane), and thus conserves the redox energy in a proton CC gradient. else case 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 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. This subunit may bind ubiquinone. 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 case and not 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; else case CC -!- CATALYTIC ACTIVITY: CC Reaction=methanophenazine + reduced coenzyme F420-(gamma-L-Glu)(n) = CC dihydromethanophenazine + H(+) + oxidized coenzyme F420-(gamma-L- CC Glu)(n); Xref=Rhea:RHEA:54752, Rhea:RHEA-COMP:12939, Rhea:RHEA- CC COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:29118, ChEBI:CHEBI:50375, CC ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.98.3; 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 is composed of at least 11 different subunits. else case or or CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. else case CC -!- SUBUNIT: NDH-1 is composed of 15 different subunits. Subunits NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. else case CC -!- SUBUNIT: The FPO complex is composed of at least 13 different subunits. CC FpoA, FpoH, FpoJ, FpoK, FpoL, FpoM and FpoN proteins constitute the CC membrane sector of the complex. else CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. end case case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- CC pass membrane protein. else case and not CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane CC protein. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. else case not defined or or CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. end case CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. XX DR PROSITE; PS00667; COMPLEX1_ND1_1; 1; trigger=no DR PROSITE; PS00668; COMPLEX1_ND1_2; 1; trigger=no DR Pfam; PF00146; NADHdh; 1; trigger=no case DR General; Transmembrane; -; 5-9; trigger=yes else DR General; Transmembrane; -; 8-9; trigger=yes end case XX KW Membrane KW Transmembrane KW Transmembrane helix case or and not KW Thylakoid else case KW Cell membrane KW Cell inner membrane else case not defined or or KW Cell membrane else case KW Cell membrane KW Cell inner membrane end case case or KW Plastoquinone KW NADP else case not and not and not KW Ubiquinone end case case not KW NAD KW Quinone KW Translocase end case XX case or GO GO:0019684; P:photosynthesis, light reaction end case case not GO GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor 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 FT None XX Size: 318-467; Related: None; Template: P26522; P29920; Q60019; P0AFD4; P42032; Scope: Bacteria Archaea; Methanosarcinales Plastid Fusion: Nter: None Cter: MF_01351 (nuoI) Duplicate: in KORVE, CYTH3, GEOMG, GEOSL, NITMU, NITOC, RHIEC, RHIME, RHOP2, RHOP5, RHOPA, RHOPB, RHOPS, CERS1, CERS4, SOLUE, SYMTH, SYNFM Plasmid: in RHIME Comments: 14 proteins form the NDH-1 complex in most bacteria whereas only 11 genes are encoded in cyanobacteria and chloroplast genomes, and 12 in archea. THET8 and PARDE are annotated with an other nomenclature. See: MEDLINE=95317406; PubMed=7796904; DOI=10.1016/0014-5793(95)00548-N; Friedrich T., Steinmuller K., Weiss H.; "The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts."; FEBS Lett. 367:107-111(1995). See: MEDLINE=98115918; PubMed=9448329; Sazanov L.A., Burrows P.A., Nixon P.J.; "The plastid ndh genes code for an NADH-specific dehydrogenase: isolation of a complex I analogue from pea thylakoid membranes."; Proc. Natl. Acad. Sci. U.S.A. 95:1319-1324(1998). See: MEDLINE=20421945; PubMed=10940377; DOI=10.1016/S0014-5793(00)01867-6; Friedrich T., Scheide D.; "The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases."; FEBS Lett. 479:1-5(2000). In some bacteria (Enterobacteriaceae, Pseudomonadaceae and Shewanellaceae), NDH-1 is made of 13 subunits as there is a fusion of subunits C and D. See: PubMed=16023073; Melo A.M., Lobo S.A., Sousa F.L., Fernandes A.S., Pereira M.M., Hreggvidsson G.O., Kristjansson J.K., Saraiva L.M., Teixeira M.; "A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus marinus complex I genes."; Biochim. Biophys. Acta 1709:95-103(2005). In Deinococcota bacteria, NDH-I is composed of 15 subunits See: PubMed=16469879; DOI=10.1126/science.1123809; Sazanov L.A., Hinchliffe P.; "Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus."; Science 311:1430-1436(2006). In NOCFA is C-terminally fused with nuoI, another subunit of the same complex. XX # Revision 1.44 2023/07/14 //