Bacterial respiratory complex I (proton-translocating NADH:quinone oxidoreductase)

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).

MODULE:bacterial_respiratory_complex_iCOMPLETECONCRETEProtein Complexmodules/bacterial_respiratory_complex_i.yaml
respiratory chain complex IGO:0045271
GO:0045271
respiratory chain complex I
GO:0045271 grounds the assembled proton-translocating respiratory complex represented by the bacterial Nuo core.
KEGG:ppu00190
Pseudomonas putida KT2440 oxidative phosphorylation
The PSEPK oxidative-phosphorylation bucket contains the contiguous PP_4119-PP_4131 nuo locus, encoding all 14 canonical Nuo subunits in 13 proteins because NuoC and NuoD are fused.
file:projects/P_PUTIDA/deep-research/PSEPK__mitochondrial_complex_i_core__ppu00190-deep-research-openscientist.md
OpenScientist review of complex I in Pseudomonas putida KT2440
Species-aware research identifies a complete, single-copy nuoA-N locus, supports the NuoC/D fusion, and distinguishes PP_0626 Ndh as a separate type-II NADH dehydrogenase rather than a complex I subunit.
PMID:34308841
Structure of Escherichia coli respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation.
Cryo-EM of the E. coli enzyme in lipid nanodiscs resolves the homologues of the 14 conserved core subunits as an L-shaped peripheral and membrane arm, with the antiporter-like NuoL, NuoM and NuoN chain and a quinone cavity formed by NuoH with NuoB and NuoD near cluster N2, grounding the E. coli exemplar set.

The 14-subunit NDH-1 core is conserved across proteobacteria and other bacterial phyla, so the module is written at the family level and grounded with two experimentally anchored gammaproteobacterial exemplar sets: the Escherichia coli K-12 NuoA-N complex, the best-characterized bacterial complex I genetically and biochemically, and the single-copy Pseudomonas putida KT2440 PP_4119-PP_4131 nuo locus. In both exemplars NuoC and NuoD are fused into one polypeptide (E. coli P33599, P. putida Q88FH5), so 13 proteins supply the 14 conserved subunit roles; in lineages with separate C and D subunits (for example Thermus thermophilus Nqo5 and Nqo4) the fused annoton is satisfied by the two polypeptides together. The fused-annoton grounding, PANTHER:PTHR11993, is the NuoD/49-kDa family; a separate NuoC/30-kDa polypeptide belongs to a different family that is not grounded here. Thermus Nqo subunits, which provided the first complete complex I structures, were not added as a third exemplar set because they would add 14 more members without adding a module role. PANTHER groundings were adopted from the module-wide grounding pass and checked against the PANTHER 19.0 member index: each exemplar falls in the cited family, except that PANTHER's own classification file places E. coli NuoF in PTHR11780:SF10 (with mitochondrial NDUFV1) while UniProt and InterPro place E. coli and P. putida NuoF in PTHR43578:SF3. The tree placement is adopted for E. coli NuoF (recorded in interpro/panther/panther-members-overrides.tsv), while P. putida NuoF, which PANTHER's files do not classify, stays in PTHR43578 by its UniProt cross-reference; the NuoF annoton is therefore grounded to both families, and the PTHR43578 and PTHR11780 reviews describe the split. NuoG is grounded at subfamily PTHR43105:SF10 rather than the family, because PTHR43105 is dominated by molybdopterin oxidoreductase catalytic subunits (nitrate reductases, formate dehydrogenases) for which a family-wide electron-transfer-subunit claim does not hold. Mitochondrial complex I, with its eukaryotic supernumerary NDUF subunits, is modelled separately (mitochondrial_complex_i_core); absence of those subunits here 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 is removed in the exemplar gene reviews rather than used to model this module. The two terms are siblings, not parent and child: in GO, GO:0008137 NADH dehydrogenase (ubiquinone) activity (RHEA:29091, EC 7.1.1.2, with 4 H+ translocated per NADH) and GO:0050136 (RHEA:46160, EC 1.6.5.9) are each is_a GO:0003954 NADH dehydrogenase activity, and GO:0008137 is not an is_a descendant of GO:0050136 (checked against the GO release in the local OAK database, 2026-11-02).

5Nodes
4Parts
0Variant Sets
0Variants
8Annotons
3Connections

Derived QC

Recommended-field compliance

100.0% recommended fields populated

All recommended fields populated.

Module deep research

✗ none found

No MODULE:bacterial_respiratory_complex_i deep-research report alongside the module YAML.

Leaf nodes lacking representative members

✓ every leaf node grounds to a representative protein.

Template conformance

✓ every declared conforms_to bundle matches its template motif.

Function consistency and core coverage

12 gene-function check(s) reflected in core functions · 0 conflict(s) · 0 evidence or coverage gap(s) (21 comparison(s))

Retained noncore functions are reported separately; they do not require promotion to core functions. Support from representative genes does not establish conservation across the whole family. Missing reviews or identifiers leave a claim unverified.

AnnotonParticipantFunctionAssessment
nuof_nadh_input nuoF (PSEPK)
UniProtKB:Q88FH3
Family Representative
NADH dehydrogenase activity
GO:0003954
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuof_nadh_input nuoF (ECOLI)
UniProtKB:P31979
Family Representative
NADH dehydrogenase activity
GO:0003954
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuoe_entry_fes nuoE (PSEPK)
UniProtKB:Q88FH4
Family Representative
electron transfer activity
GO:0009055
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuoe_entry_fes nuoE (ECOLI)
UniProtKB:P0AFD1
Family Representative
electron transfer activity
GO:0009055
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuog_fes_relay nuoG (PSEPK)
UniProtKB:Q88FH2
Family Representative
electron transfer activity
GO:0009055
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuog_fes_relay nuoG (ECOLI)
UniProtKB:P33602
Family Representative
electron transfer activity
GO:0009055
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuob_terminal_fes nuoB (PSEPK)
UniProtKB:Q88FH6
Family Representative
electron transfer activity
GO:0009055
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuob_terminal_fes nuoB (ECOLI)
UniProtKB:P0AFC7
Family Representative
electron transfer activity
GO:0009055
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuocd_quinone_site nuoC (PSEPK)
UniProtKB:Q88FH5
Family Representative
quinone binding
GO:0048038
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuocd_quinone_site nuoC (ECOLI)
UniProtKB:P33599
Family Representative
quinone binding
GO:0048038
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuoi_fes_relay nuoI (PSEPK)
UniProtKB:Q88FH0
Family Representative
electron transfer activity
GO:0009055
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuoi_fes_relay nuoI (ECOLI)
UniProtKB:P0AFD6
Family Representative
electron transfer activity
GO:0009055
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
nuoahjk_interface_subunits PROTEIN_COMPLEX
Gene
proton transmembrane transporter activity
GO:0015078
Participant Unchecked
No direct UniProt participant to compare. Abstract selectors and complex-wide activities cannot be inferred from donor or subunit gene reviews.
nuolmn_proton_pump PROTEIN_COMPLEX
Gene
proton transmembrane transporter activity
GO:0015078
Participant Unchecked
No direct UniProt participant to compare. Abstract selectors and complex-wide activities cannot be inferred from donor or subunit gene reviews.
nuof_nadh_input NuoF/Nqo1/NDUFV1 family
PANTHER:PTHR43578
Family
NADH dehydrogenase activity
GO:0003954
Family Supported
Family review supports GO:0003954 FAMILY_WIDE. NADH oxidation at the FMN of the 51 kDa-type flavin module is shared by the complex I NuoF members (experimentally in E. coli NuoF) and by the NAD+-reducing hydrogenase and formate-dehydrogenase flavoprotein subunits, which catalyse the same NADH/NAD+ exchange (GO:0003954 is defined without direction-specific acceptor). The nuo locus itself was found with probes from the conserved NAD(H)-binding subunit shared by complex I and the NAD+-reducing hydrogenase. Two members are recorded as exceptions: the truncated ferredoxin P07324, and HndC, whose NADP specificity would put it outside this NADH-specific term.
nuof_nadh_input NuoF/Nqo1/NDUFV1 family
PANTHER:PTHR11780
Family
NADH dehydrogenase activity
GO:0003954
Family Supported
Family review supports GO:0003954 FAMILY_WIDE. The subunit's own chemistry, with the acceptor left unspecified: NADH docks on the glycine-rich loop (UniProt binding site 87-96 of P49821, GRGGAGFPTG, conserved in bacteria, plants, fungi and animals) and transfers a hydride to the bound FMN. This is true of every member, respiratory compartment and quinone identity aside, and it is the term a PAINT curator should place at the family root. PAINT currently asserts it only at the bacterial node PTN000207323, which is why human NDUFV1 - and every other eukaryotic member - receives no molecular-function IBA at all despite this being the single best-characterised function in the family.
nuoe_entry_fes NuoE/Nqo2/NDUFV2 family
PANTHER:PTHR10371
Family
electron transfer activity
GO:0009055
Family Supported
Family review supports GO:0009055 FAMILY_WIDE. The subunit's own molecular function: redox exchange through its [2Fe-2S] cluster N1a with the reduced FMN of the 51 kDa subunit. The four cysteine ligands and the cluster domain (NCBIfam TIGR01958, PIRSF000216, PROSITE PS01099) are conserved across the reviewed members, and rapid NADH-driven reduction of N1a is measured in E. coli complex I. The cluster is on a side path rather than the main wire, so the term asserts electron exchange, not a position on the FMN-to-quinone pathway. Applies equally to the S. pombe homologue, which keeps the cluster domain even without a complex I.
nuog_fes_relay NuoG/Nqo3/NDUFS1 family
PANTHER:PTHR43105:SF10
Family
electron transfer activity
GO:0009055
Family Supported
Family review supports GO:0009055 for PANTHER:PTHR43105:SF10. For the complex I 75 kDa subunits electron transfer through their iron-sulfur clusters is the subunit's own function (E. coli NuoG clusters N1b, N4, N5 on the main path). For the molybdoenzyme majority the defining function is substrate-specific catalysis at the Mo/W cofactor; their clusters do move electrons, so the term is not wrong there, but it does not describe the family's shared function and is asserted here only for the complex I subfamilies. SF10 is mixed (it also holds AioA, IdrA and assimilatory nitrate reductases, which are themselves Fe-S redox enzymes), so the grant is safe for all its members though informative mainly for NuoG.
nuob_terminal_fes NuoB/Nqo6/NDUFS7 family
PANTHER:PTHR11995
Family
electron transfer activity
GO:0009055
Family Supported
Family review supports GO:0009055 FAMILY_WIDE. Every characterised member is the terminal iron-sulfur subunit of a complex I-type enzyme (bacterial NDH-1 NuoB, mitochondrial NDUFS7, chloroplast NDH NdhK) and carries the conserved four-cysteine motif (Pfam Oxidored_q6, PROSITE COMPLEX1_20K) that ligates the [4Fe-4S] cluster N2, which passes electrons from the iron-sulfur chain to the bound quinone. The electron donor upstream differs (NADH versus ferredoxin) but the subunit's own electron-transfer role does not, so the term is safe family-wide, unlike the NADH-specific GO:0008137. The minor subfamilies SF33 (second NuoB copies) and SF22 (mitochondrial NDUFS7) retain the same motif family assignment; no member is known to have lost the cluster.
nuocd_quinone_site NuoC-NuoD/Nqo5-Nqo4/NDUFS3-NDUFS2 families
PANTHER:PTHR11993
Family
quinone binding
GO:0048038
Family Supported
Family review supports GO:0048038 FAMILY_WIDE. Every member of the family, respiratory and plastid alike, builds the chamber in which a quinone is reduced, and the His/Tyr pair that contacts the headgroup is invariant across animals, plants, plastids and bacteria (see the quinone_channel_his_tyr site). The term names the chemistry without naming the acceptor, which is precisely the granularity at which this family is coherent. This is also the term a future PAINT curator could safely place at the family root: no node in the current PTHR11993 PAINT slice asserts any quinone-binding term at all, although the quinone channel is the defining structural contribution of the subunit.
nuoi_fes_relay NuoI/Nqo9/NDUFS8 family
PANTHER:PTHR10849
Family
electron transfer activity
GO:0009055
Family Supported
Family review supports GO:0009055 FAMILY_WIDE. Every member has two cysteine-ligated 4Fe-4S ferredoxin-type domains and is the two-cluster relay segment of a complex-I-like electron path. In complex I the clusters bridge N5 and N2, and the homologous FHL, hydrogenase-4 and F420H2 dehydrogenase subunits occupy the equivalent relay position. Electron transfer through the subunit's own clusters is the shared activity, whatever the donor and acceptor of the parent complex.

Gene-review completeness (26/26 grounded genes reviewed)

26 complete review(s) · 1 with deep research · 0 missing review · 25 reviewed but lacking deep research

Gene Review Complete Deep research
nuoA P0AFC3 ✓ ✓ ✗
nuoA Q88FH7 ✓ ✓ ✗
nuoB P0AFC7 ✓ ✓ ✗
nuoB Q88FH6 ✓ ✓ ✗
nuoC P33599 ✓ ✓ ✗
nuoC Q88FH5 ✓ ✓ ✗
nuoE P0AFD1 ✓ ✓ ✗
nuoE Q88FH4 ✓ ✓ ✗
nuoF P31979 ✓ ✓ ✗
nuoF Q88FH3 ✓ ✓ ✓
nuoG P33602 ✓ ✓ ✗
nuoG Q88FH2 ✓ ✓ ✗
nuoH P0AFD4 ✓ ✓ ✗
nuoH Q88FH1 ✓ ✓ ✗
nuoI P0AFD6 ✓ ✓ ✗
nuoI Q88FH0 ✓ ✓ ✗
nuoJ P0AFE0 ✓ ✓ ✗
nuoJ Q88FG9 ✓ ✓ ✗
nuoK P0AFE4 ✓ ✓ ✗
nuoK Q88FG8 ✓ ✓ ✗
nuoL P33607 ✓ ✓ ✗
nuoL Q88FG7 ✓ ✓ ✗
nuoM P0AFE8 ✓ ✓ ✗
nuoM Q88FG6 ✓ ✓ ✗
nuoN P0AFF0 ✓ ✓ ✗
nuoN Q88FG5 ✓ ✓ ✗

Details

Context
bacteriaNCBITaxon:2
Bacterial respiratory complex IProtein Complexbacterial_respiratory_complex_i
respiratory chain complex IGO:0045271
Context
bacteriaNCBITaxon:2

Connections

nuo_n_module -> nuo_q_module Provides Input For
Electrons accepted from NADH at FMN flow through the peripheral-arm iron-sulfur relay to the quinone-reduction module.
Quinone-site redox chemistry drives conformational changes at the peripheral-arm/membrane-arm interface.
The proximal membrane interface transmits redox-linked conformational changes to the antiporter-like proton-pumping subunits.
Part 1: NADH oxidation and entry electron transfer
Nuo N-module NADH-input armProtein Complexnuo_n_module

Soluble peripheral-arm segment in which NuoF oxidizes NADH at FMN and NuoE and NuoG relay electrons through iron-sulfur centers.

Annotons

NuoF FMN-dependent NADH-input subunit
nuof_nadh_input
Participant: Family: NuoF/Nqo1/NDUFV1 family
Family:
NuoF/Nqo1/NDUFV1 family
Representative Members: nuoF (PSEPK)UniProtKB:Q88FH3 nuoF (ECOLI)UniProtKB:P31979

Function

NADH dehydrogenase activityGO:0003954
Substrates: NADH FMN
Products: NAD+ reduced FMN (FMNH2)
Cofactors: FMN

Catalytic entry subunit that binds FMN and accepts a hydride from NADH before passing electrons into the iron-sulfur relay.

NuoE entry iron-sulfur subunit
nuoe_entry_fes
Participant: Family: NuoE/Nqo2/NDUFV2 family
Family:
NuoE/Nqo2/NDUFV2 familyPANTHER:PTHR10371
Representative Members: nuoE (PSEPK)UniProtKB:Q88FH4 nuoE (ECOLI)UniProtKB:P0AFD1

Function

electron transfer activityGO:0009055

Small iron-sulfur subunit at the NADH-input end of the peripheral arm.

NuoG iron-sulfur relay subunit
nuog_fes_relay
Participant: Family: NuoG/Nqo3/NDUFS1 family
Family:
NuoG/Nqo3/NDUFS1 familyPANTHER:PTHR43105:SF10
Representative Members: nuoG (PSEPK)UniProtKB:Q88FH2 nuoG (ECOLI)UniProtKB:P33602

Function

electron transfer activityGO:0009055
Cofactors: 2Fe-2S cluster 4Fe-4S clusters

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 exemplar subunits.

Part 2: terminal iron-sulfur relay and quinone-site architecture
Nuo Q-module quinone-reduction armProtein Complexnuo_q_module

Peripheral-arm segment that completes the iron-sulfur wire and forms the quinone-reactive cavity at the membrane-arm junction.

Annotons

NuoB terminal iron-sulfur subunit
nuob_terminal_fes
Participant: Family: NuoB/Nqo6/NDUFS7 family
Family:
NuoB/Nqo6/NDUFS7 familyPANTHER:PTHR11995
Representative Members: nuoB (PSEPK)UniProtKB:Q88FH6 nuoB (ECOLI)UniProtKB:P0AFC7

Function

electron transfer activityGO:0009055
Cofactors: 4 iron, 4 sulfur clusterGO:0051539

Carries the terminal iron-sulfur center that supplies electrons to quinone at the Q-site.

Fused NuoC/D quinone-site scaffold
nuocd_quinone_site
Participant: Family: NuoC-NuoD/Nqo5-Nqo4/NDUFS3-NDUFS2 families
Family:
NuoC-NuoD/Nqo5-Nqo4/NDUFS3-NDUFS2 familiesPANTHER:PTHR11993
Representative Members: nuoC (PSEPK)UniProtKB:Q88FH5 nuoC (ECOLI)UniProtKB:P33599

Function

quinone bindingGO:0048038

Forms the quinone-cavity scaffold. In E. coli, P. putida and many other Gammaproteobacteria the C and D subunits are fused into one polypeptide; elsewhere they are separate subunits.

NuoI iron-sulfur relay subunit
nuoi_fes_relay
Participant: Family: NuoI/Nqo9/NDUFS8 family
Family:
NuoI/Nqo9/NDUFS8 familyPANTHER:PTHR10849
Representative Members: nuoI (PSEPK)UniProtKB:Q88FH0 nuoI (ECOLI)UniProtKB:P0AFD6

Function

electron transfer activityGO:0009055
Cofactors: 4 iron, 4 sulfur clusterGO:0051539

Iron-sulfur subunit in the distal portion of the relay leading toward the terminal quinone-reducing center.

Part 3: peripheral-arm to membrane-arm coupling interface
Nuo membrane coupling interfaceProtein Complexnuo_membrane_interface

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.

Annotons

NuoA/NuoH/NuoJ/NuoK membrane-interface subunits
nuoahjk_interface_subunits
Participant: Protein Complex: NuoA-NuoH-NuoJ-NuoK membrane-interface unit
Protein Complex:
NuoA-NuoH-NuoJ-NuoK membrane-interface unit
Active units:
NuoA membrane-interface subunit
Participant: Family: NuoA-family small membrane subunit
Family:
NuoA-family small membrane subunitPANTHER:PTHR11058
Representative Members: nuoA (PSEPK)UniProtKB:Q88FH7 nuoA (ECOLI)UniProtKB:P0AFC3
NuoH membrane-interface subunit
Participant: Family: NuoH/ND1 family
Family:
NuoH/ND1 familyPANTHER:PTHR11432
Representative Members: nuoH (PSEPK)UniProtKB:Q88FH1 nuoH (ECOLI)UniProtKB:P0AFD4
Role: Membrane-arm subunit at the junction with the peripheral arm. With NuoB and NuoD it forms the quinone-binding cavity (Q-cavity) that leads from the membrane to the quinone-headgroup site near cluster N2, and it also carries a five-helix repeat like that of the antiporter-like subunits.
NuoJ membrane-interface subunit
Participant: Family: NuoJ/ND6 family
Family:
NuoJ/ND6 familyPANTHER:PTHR33269
Representative Members: nuoJ (PSEPK)UniProtKB:Q88FG9 nuoJ (ECOLI)UniProtKB:P0AFE0
NuoK membrane-interface subunit
Participant: Family: NuoK/ND4L family
Family:
NuoK/ND4L familyPANTHER:PTHR11434
Representative Members: nuoK (PSEPK)UniProtKB:Q88FG8 nuoK (ECOLI)UniProtKB:P0AFE4

Function

proton transmembrane transporter activityGO:0015078
Substrates: H+ (cytoplasmic side)
Products: H+ (periplasmic side)

Locations

plasma membraneGO:0005886

Membrane-embedded coupling interface between quinone chemistry and the distal antiporter-like proton-translocation machinery.

Part 4: antiporter-like proton-pumping membrane arm
NuoL/NuoM/NuoN antiporter-like armProtein Complexnuo_antiporter_arm

Three homologous long membrane subunits form the distal membrane arm and are required for vectorial proton translocation by complex I.

Annotons

NuoL/NuoM/NuoN antiporter-like subunits
nuolmn_proton_pump
Participant: Protein Complex: NuoL-NuoM-NuoN antiporter-like unit
Protein Complex:
NuoL-NuoM-NuoN antiporter-like unit
Active units:
NuoL antiporter-like subunit
Participant: Family: NuoL/ND5 antiporter-like family
Family:
NuoL/ND5 antiporter-like familyPANTHER:PTHR42829
Representative Members: nuoL (PSEPK)UniProtKB:Q88FG7 nuoL (ECOLI)UniProtKB:P33607
NuoM antiporter-like subunit
Participant: Family: NuoM/ND4 antiporter-like family
Family:
NuoM/ND4 antiporter-like familyPANTHER:PTHR43507
Representative Members: nuoM (PSEPK)UniProtKB:Q88FG6 nuoM (ECOLI)UniProtKB:P0AFE8
NuoN/ND2 antiporter-like subunit
Participant: Family: NuoN/ND2 antiporter-like family
Family:
NuoN/ND2 antiporter-like familyPANTHER:PTHR22773
Representative Members: nuoN (PSEPK)UniProtKB:Q88FG5 nuoN (ECOLI)UniProtKB:P0AFF0

Function

proton transmembrane transporter activityGO:0015078
Substrates: H+ (cytoplasmic side)
Products: H+ (periplasmic side)

Locations

plasma membraneGO:0005886

Distal membrane-arm unit that converts redox-linked conformational changes into proton translocation.