ExPASy Proteomics Server

Accession	MF_01350
Dates	24-MAY-2006 (Created) 30-NOV-2009 (Last updated, Version 23)

Data class

Protein

Predictors

HAMAP; MF_01350_B; [distribution of match scores in UniProtKB];[seed alignment for MF_01350_B]

Predictors

HAMAP; MF_01350_A; [distribution of match scores in UniProtKB];[seed alignment for MF_01350_A]

Names

NDH1_NuoH

Identifier

NU1C

Protein name

RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic; EC=1.6.5.-; AltName: Full=NAD(P)H dehydrogenase subunit 1; Short=NDH subunit 1; AltName: Full=NADH-plastoquinone oxidoreductase subunit 1;

Gene name

ndhA

Identifier

NU1C

Protein name

RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1; EC=1.6.5.-; AltName: Full=NAD(P)H dehydrogenase I subunit 1; AltName: Full=NDH-1 subunit 1; AltName: Full=NDH-A;

Gene name

ndhA

Identifier

FPOH

Protein name

RecName: Full=F(420)H(2) oxidoreductase subunit H; AltName: Full=F(420)H(2) dehydrogenase subunit H; AltName: Full=FPO subunit H;

Gene name

fpoH

Identifier

NUOH

Protein name

RecName: Full=NADH-quinone oxidoreductase subunit H; EC=1.6.99.5; AltName: Full=NADH dehydrogenase I subunit H; AltName: Full=NDH-1 subunit H;

Gene name

nuoH

FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).

FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).

FUNCTION: FPO shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to quinones in the F(420)H(2):heterodisulfide oxidoreduction chain. The immediate electron acceptor for the enzyme in this species is believed to be methanophenazine. Couples the redox reaction to proton translocation (for every two electrons transferred, 0.9 hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).

FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).

FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone (By similarity).

CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + plastoquinol.

CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.

SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus (By similarity).

SUBUNIT: NDH-1 is composed of at least 11 different subunits (By similarity).

SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits nuoA, H, J, K, L, M, N constitute the membrane sector of the complex (By similarity).

SUBUNIT: NDH-1 is composed of 15 different subunits. Subunits nuoA, H, J, K, L, M, N constitute the membrane sector of the complex (By similarity).

SUBUNIT: FPO is composed of at least 12 different subunits. Subunits fpoA, H, J, K, L, M, N constitute the membrane sector of the complex (By similarity).

SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits nuoA, H, J, K, L, M, N constitute the membrane sector of the complex (By similarity).

SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein (By similarity).

SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein (Potential).

SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein (By similarity).

SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein (Potential).

SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein (Potential).

SIMILARITY: Belongs to the complex I subunit 1 family.

PROSITE	PS00667; COMPLEX1_ND1_1; 1; PS00668; COMPLEX1_ND1_2; 1;
Pfam	PF00146; NADHdh; 1;

General

Transmembrane; -; 5-9; trigger=Yes;

General

Transmembrane; -; 8-9; trigger=Yes;

Membrane, Oxidoreductase, Quinone, Transmembrane.

Thylakoid.

Cell membrane, Cell inner membrane.

Cell membrane.

Plastoquinone, NADP.

Ubiquinone.

FAD.

NAD.

GO:0055114; Biological process: oxidation reduction.

GO:0019684; Biological process: photosynthesis, light reaction.

GO:0016655; Molecular function: oxidoreductase activity, acting on NADH or NADPH, quinone or similar compound as acceptor.

GO:0009535; Cellular component: chloroplast thylakoid membrane.

GO:0005886; Cellular component: plasma membrane.

GO:0042651; Cellular component: thylakoid membrane.

GO:0005886; Cellular component: plasma membrane.

GO:0005886; Cellular component: plasma membrane.

Size range:	318-467 amino acids
Related UniRules:	None
Template:	P26522 (NU1C_SYNY3); P29920 (NQO8_PARDE); Q60019 (NQO8_THET8); P0AFD4 (NUOH_ECOLI); P42032 (NUOH_RHOCA): [Recover all]
Scope:	Bacteria Archaea; Methanosarcinales Plastid
Fusion:	Nter: None; Cter: MF_01351 (nuoI)
Duplicate:	in ACIBL, CYTH3, GEOMG, GEOSL, NITMU, NITOC, RHIEC, RHIME, RHOP2, RHOP5, RHOPA, RHOPB, RHOPS, RHOS1, RHOS4, SOLUE, SYMTH, SYNFM
Plasmid encoded:	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 Deinococcus-Thermus 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.