HAMAP rule MF_01394
General rule information
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| Accession | MF_01394 |
| Dates | 28-NOV-2008 (Created) 17-FEB-2023 (Last updated, Version 25) |
| Name | NDH1_NuoA |
| Scope | Bacteria
Plastid |
| Templates | P0AFC3 (NUOA_ECOLI); P19045 (NU3C_SYNY3); Q8DJ02 (NU3C_THEVB): [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
| 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. Cyanobacteriotal NDH-1 also plays a role in inorganic carbon-concentration. |
else case <OC:Actinomycetota> or <OC:Bacteroidota> or <OC:Chlorobiota> or <OC:Deinococcota> or <OC:Bacillota>
| 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 a 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. |
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
| 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 can be composed of about 15 different subunits; different subcomplexes with different compositions have been identified which probably have different functions. |
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
| 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>
| 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 3 family. |
Keywords
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case <OG:Chloroplast> or <OC:Cyanobacteriota>
else case not <OC:Actinomycetota> and not <OC:Bacteroidota> and not <OC:Chlorobiota> and not <OC:Deinococcota> and not <OC:Bacillota>
end case
case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter>
else case <OC:Gloeobacter>
else case not defined <Property:Membrane> or <Property:Membrane=1>
else case <Property:Membrane=2>
end case
Gene Ontology
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case <OG:Chloroplast> or <OC:Cyanobacteriota>
GO:0016655; Molecular function: oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor.
GO:0019684; Biological process: photosynthesis, light reaction.
GO:0019684; Biological process: photosynthesis, light reaction.
else
GO:0050136; Molecular function: NADH dehydrogenase (quinone) activity.
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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| Pfam | PF00507; Oxidored_q4; 1; |
Computed features
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| General | Transmembrane; -; 3; trigger=yes; |
Additional information
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| Size range | 116-211 amino acids |
| Related rules | None |
| Fusion | None |
| Comments | THEVB has a proven longer N-terminus than the predictions for some other cyanobacteria; left it and a few others longer. 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. |