AC MF_01456; DC Protein; auto TR HAMAP; MF_01456; -; 1; level=0 XX Names: NDH1_NuoK XX case ID NU4LC DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic; DE EC=7.1.1.-; DE AltName: Full=NAD(P)H dehydrogenase subunit 4L; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 4L; GN Name=ndhE; else case ID NU4LC DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 4L; DE EC=7.1.1.-; DE AltName: Full=NAD(P)H dehydrogenase subunit 4L; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 4L; DE AltName: Full=NDH-1, subunit 4L; DE AltName: Full=NDH-E; GN Name=ndhE; else ID NUOK DE RecName: Full=NADH-quinone oxidoreductase subunit K; DE EC=7.1.1.-; DE AltName: Full=NADH dehydrogenase I subunit K; DE AltName: Full=NDH-1 subunit K; GN Name=nuoK; 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 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 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 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 4L family. XX DR Pfam; PF00420; Oxidored_q2; 1; trigger=no DR General; Transmembrane; -; 3; trigger=yes 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 Transmembrane 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 KW Transmembrane helix 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 FT None XX Size: 93-148; Related: None; Template: P0AFE4; Q56226; P29923; Scope: Bacteria Plastid Fusion: Nter: None Cter: None Duplicate: in KORVE, AQUAE, CITBB, GEOMG, GEODF, GEOSL, GEOSM, GEOUR, RHIE6, RHIEC, RHIME, SINFN, RHOPA, SINMW, SOLUE, STRAW, STRCO, STRGG, SYMTH, SYNFM Plasmid: in 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. XX # Revision 1.26 2023/06/15 //