HAMAP rule MF_01350
General rule information
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Accession | MF_01350 |
Dates | 24-MAY-2006 (Created)
14-JUL-2023 (Last updated, Version 44) |
Name | NDH1_NuoH |
Scope(s) |
Bacteria Archaea Methanosarcinales Plastid |
Template(s) | P26522 (NU1C_SYNY3); P29920 (NQO8_PARDE); Q60019 (NQO8_THET8); P0AFD4 (NUOH_ECOLI); P42032 (NUOH_RHOCA); [ Recover all ] |
Triggered by |
HAMAP; MF_01350 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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case <OG:Chloroplast> | |
Identifier | NU1C |
Protein name | RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic; EC=7.1.1.-; AltName: Full=NAD(P)H dehydrogenase subunit 1; Short=NDH subunit 1; AltName: Full=NADH-plastoquinone oxidoreductase subunit 1; |
Gene name | Name=ndhA; |
else case <OC:Cyanobacteriota> | |
Identifier | NU1C |
Protein name | RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1; EC=7.1.1.-; AltName: Full=NAD(P)H dehydrogenase I subunit 1; AltName: Full=NDH-1 subunit 1; AltName: Full=NDH-A; |
Gene name | Name=ndhA; |
else case <OC:Methanomicrobia> | |
Identifier | FPOH |
Protein name | RecName: Full=F(420)H(2) dehydrogenase subunit H; EC=1.5.98.3; AltName: Full=F(420)H(2)-dependent phenazine dehydrogenase subunit H; AltName: Full=F(420)H(2)-dependent phenazine oxidoreductase subunit H; Short=FPO subunit H; |
Gene name | Name=fpoH; |
else | |
Identifier | NUOH |
Protein name | RecName: Full=NADH-quinone oxidoreductase subunit H; EC=7.1.1.-; AltName: Full=NADH dehydrogenase I subunit H; AltName: Full=NDH-1 subunit H; |
Gene name | Name=nuoH; |
end case |
Comments
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case <OG:Chloroplast> | |
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. |
else case <OC:Cyanobacteriota> | |
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. |
else case <OC:Methanomicrobia> | |
FUNCTION | Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
else case <OC:Mycobacterium> or <OC:Rhodothermus> | |
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. |
else | |
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. |
end case | |
case <OG:Chloroplast> or <OC:Cyanobacteriota> | |
CATALYTIC ACTIVITY | Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192; |
CATALYTIC ACTIVITY | Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192; |
else case <OC:Bacteria> and not <OC:Cyanobacteriota> | |
CATALYTIC ACTIVITY | Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; |
else case <OC:Methanomicrobia> | |
CATALYTIC ACTIVITY | Reaction=methanophenazine + reduced coenzyme F420-(gamma-L-Glu)(n) = dihydromethanophenazine + H(+) + oxidized coenzyme F420-(gamma-L- Glu)(n); Xref=Rhea:RHEA:54752, Rhea:RHEA-COMP:12939, Rhea:RHEA- COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:29118, ChEBI:CHEBI:50375, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.98.3; |
end case | |
case <OG:Chloroplast> | |
SUBUNIT | NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus. |
else case <OC:Cyanobacteriota> | |
SUBUNIT | NDH-1 is composed of at least 11 different subunits. |
else case <OC:Enterobacterales> or <OC:Shewanellaceae> or <OC:Pseudomonadaceae> | |
SUBUNIT | NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex. |
else case <OC:Deinococci> | |
SUBUNIT | NDH-1 is composed of 15 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex. |
else case <OC:Methanomicrobia> | |
SUBUNIT | The FPO complex is composed of at least 13 different subunits. FpoA, FpoH, FpoJ, FpoK, FpoL, FpoM and FpoN proteins constitute the membrane sector of the complex. |
else | |
SUBUNIT | NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex. |
end case | |
case <OG:Chloroplast> | |
SUBCELLULAR LOCATION | Plastid, chloroplast thylakoid membrane; Multi- pass membrane protein. |
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter> | |
SUBCELLULAR LOCATION | Cellular thylakoid membrane; Multi-pass membrane protein. |
else case <OC:Gloeobacter> | |
SUBCELLULAR LOCATION | Cell inner membrane; Multi-pass membrane protein. |
else case not defined <Property:Membrane> or <Property:Membrane=1> or <OC:Archaea> | |
SUBCELLULAR LOCATION | Cell membrane; Multi-pass membrane protein. |
else case <Property:Membrane=2> | |
SUBCELLULAR LOCATION | Cell inner membrane; Multi-pass membrane protein. |
end case | |
SIMILARITY | Belongs to the complex I subunit 1 family. |
Keywords
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Membrane | |
Transmembrane | |
Transmembrane helix | |
case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter> | |
Thylakoid | |
else case <OC:Gloeobacter> | |
Cell membrane | |
Cell inner membrane | |
else case not defined <Property:Membrane> or <Property:Membrane=1> or <OC:Archaea> | |
Cell membrane | |
else case <Property:Membrane=2> | |
Cell membrane | |
Cell inner membrane | |
end case | |
case <OG:Chloroplast> or <OC:Cyanobacteriota> | |
Plastoquinone | |
NADP | |
else case not <OC:Mycobacterium> and not <OC:Rhodothermus> and not <OC:Archaea> | |
Ubiquinone | |
end case | |
case not <OC:Methanomicrobia> | |
NAD | |
Quinone | |
<a href="https://www.uniprot.org/keywords/KW-1278">Translocase</a> | |
end case |
Gene Ontology
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case <OCellular component:Cyanobacteriota> or <OG:Chloroplast> | |
GO:0019684; Biological process:photosynthesis, light reaction | |
end case | |
case not <OCellular component:Archaea> | |
GO:0016655; Molecular function:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor | |
end case | |
case <OCellular component:Cyanobacteriota> and not <OC:Gloeobacter> | |
GO:0042651; Cellular component:thylakoid membrane | |
else case <OG:Chloroplast> | |
GO:0009535; Cellular component:chloroplast thylakoid membrane | |
else; https://www.ebi.ac.uk/QuickGO/term/else | |
GO:0005886; Cellular component:plasma membrane | |
end case |
Cross-references
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PROSITE | PS00667; COMPLEX1_ND1_1; 1; |
PROSITE | PS00668; COMPLEX1_ND1_2; 1; |
Pfam | PF00146; NADHdh; 1; |
General | Transmembrane; -; 5-9; |
General | Transmembrane; -; 8-9; |
Features
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Additional information
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Size range | 318-467 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: MF_01351 (nuoI) |
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. |