Function
Catalytic entry subunit that binds FMN and accepts a hydride from NADH before passing electrons into the iron-sulfur relay.
Reusable bacterial module for the conserved 14-subunit respiratory complex I, also called NDH-1 or NADH:quinone oxidoreductase. The peripheral arm oxidizes NADH, transfers electrons through FMN and iron-sulfur centers, and reduces the quinone pool. The membrane arm couples this redox chemistry to proton translocation. The module separates the NADH-input, quinone-reduction, membrane-interface, and antiporter-like proton-pumping parts so that fused subunits such as NuoC/D can be represented without collapsing the enzyme to a single step. It excludes the non-homologous, non-proton-pumping type-II NADH dehydrogenase (Ndh/NDH-2).
Pseudomonas putida KT2440 supplies exact representatives for every bacterial core subunit. PP_4121/Q88FH5 is a single NuoC/D polypeptide and therefore satisfies both conserved C- and D-subunit roles. Eukaryotic supernumerary NDUF subunits are outside this bacterial core module and their absence is not a pathway hole. GO:0050136 denotes non-electrogenic NADH:quinone activity and is incompatible with the defining proton-translocating chemistry of NDH-1; its automated propagation to Nuo subunits should be removed rather than used to model this module.
All recommended fields populated.
✗ none found
No MODULE:bacterial_respiratory_complex_i deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
13 complete review(s) · 1 with deep research · 0 missing review · 12 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| nuoA Q88FH7 | ✓ | ✓ | ✗ |
| nuoB Q88FH6 | ✓ | ✓ | ✗ |
| nuoC Q88FH5 | ✓ | ✓ | ✗ |
| nuoE Q88FH4 | ✓ | ✓ | ✗ |
| nuoF Q88FH3 | ✓ | ✓ | ✓ |
| nuoG Q88FH2 | ✓ | ✓ | ✗ |
| nuoH Q88FH1 | ✓ | ✓ | ✗ |
| nuoI Q88FH0 | ✓ | ✓ | ✗ |
| nuoJ Q88FG9 | ✓ | ✓ | ✗ |
| nuoK Q88FG8 | ✓ | ✓ | ✗ |
| nuoL Q88FG7 | ✓ | ✓ | ✗ |
| nuoM Q88FG6 | ✓ | ✓ | ✗ |
| nuoN Q88FG5 | ✓ | ✓ | ✗ |
Soluble peripheral-arm segment in which NuoF oxidizes NADH at FMN and NuoE and NuoG relay electrons through iron-sulfur centers.
Catalytic entry subunit that binds FMN and accepts a hydride from NADH before passing electrons into the iron-sulfur relay.
Small iron-sulfur subunit at the NADH-input end of the peripheral arm.
Large peripheral-arm iron-sulfur protein that relays electrons away from the FMN-containing input site using one 2Fe-2S and three 4Fe-4S clusters in the PSEPK exemplar.
Peripheral-arm segment that completes the iron-sulfur wire and forms the quinone-reactive cavity at the membrane-arm junction.
Carries the terminal iron-sulfur center that supplies electrons to quinone at the Q-site.
Forms the quinone-cavity scaffold. In many Gammaproteobacteria, including P. putida KT2440, the C and D subunits are fused.
Iron-sulfur subunit in the distal portion of the relay leading toward the terminal quinone-reducing center.
Conserved small membrane subunits and NuoH form the proximal membrane arm around the quinone site and transmit redox-linked conformational changes into the proton-pumping arm.
Membrane-embedded coupling interface between quinone chemistry and the distal antiporter-like proton-translocation machinery.
Three homologous long membrane subunits form the distal membrane arm and are required for vectorial proton translocation by complex I.
Distal membrane-arm unit that converts redox-linked conformational changes into proton translocation.