HAMAP rule MF_01350
General rule information
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| Accession | MF_01350 |
| Dates | 24-MAY-2006 (Created) 17-FEB-2023 (Last updated, Version 43) |
| Name | NDH1_NuoH |
| Scope | Bacteria
Archaea; Methanosarcinales
Plastid |
| Templates | P26522 (NU1C_SYNY3); P29920 (NQO8_PARDE); Q60019 (NQO8_THET8); P0AFD4 (NUOH_ECOLI); P42032 (NUOH_RHOCA): [Recover all] |
| Triggered by |
Propagated annotation
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Identifier, protein and gene names
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case <OG:Chloroplast>
| Identifier |
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| Protein name |
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| Gene name |
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else case <OC:Cyanobacteriota>
| Identifier |
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| Protein name |
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| Gene name |
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else case <OC:Methanomicrobia>
| Identifier |
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| Protein name |
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| Gene name |
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else
| Identifier |
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| Protein name |
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| Gene name |
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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 | 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. |
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 | RHEA:42608: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+) |
| RHEA:42612: a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n H(+)(out) + NADP(+) |
else case <OC:Bacteria> and not <OC:Cyanobacteriota>
| Catalytic activity | RHEA:57888: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) |
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 | FPO is composed of at least 12 different subunits. Subunits FpoA, H, J, K, L, M, N 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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case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter>
else case <OC:Gloeobacter>
else case not defined <Property:Membrane> or <Property:Membrane=1> or <OC:Archaea>
else case <Property:Membrane=2>
end case
case <OG:Chloroplast> or <OC:Cyanobacteriota>
else case not <OC:Mycobacterium> and not <OC:Rhodothermus> and not <OC:Archaea>
end case
case <OC:Methanosarcinales>
else
end case
Gene Ontology
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case <OC:Cyanobacteriota> or <OG:Chloroplast>
GO:0019684; Biological process: photosynthesis, light reaction.
end case
case not <OC:Archaea>
GO:0016655; Molecular function: oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor.
end case
case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
GO:0042651; Cellular component: thylakoid membrane.
else case <OG:Chloroplast>
GO:0009535; Cellular component: chloroplast thylakoid membrane.
else
GO:0005886; Cellular component: plasma membrane.
end case
Cross-references
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Computed features
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case <OG:Chloroplast>
| General | Transmembrane; -; 5-9; trigger=yes; |
else
| Transmembrane; -; 8-9; trigger=yes; |
end case
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. |