nuoF Family assigned · medium auto-curated

H37Rv Rv3150 · MTBC0 mtbc0_003348 · 445 aa · 3538114–3539451 (+) · RefSeq NP_217666.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)NADH-quinone oxidoreductase subunit F
MTBC0 PGAP re-annotationNADH-quinone oxidoreductase subunit NuoF
Revised (this work)NADH-quinone oxidoreductase subunit NuoF. Pfam: Complex1_51K (PF01512.23), SLBB (PF10531.16), NADH_4Fe-4S (PF10589.15).

Auto-curated: this verdict and function were generated by rules from PGAP + Pfam + Foldseek and have not been hand-reviewed.

Curated reference (UniProt)

UniProt P9WIV7 SwissProt · reviewed · Evidence at protein level
UniProt nameNADH-quinone oxidoreductase subunit F
EC (curated) EC 7.1.1.-
Curated functionNDH-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 (By similarity).

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category C Energy production and conversion
Preferred namenuoF
eggNOG descriptionNDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain
Orthologous groupCOG1894
EC number EC 1.6.5.3
KEGG orthology K00335
KEGG pathways map00190, map01100
KEGG modules M00144

Orthology-based transfer (eggNOG 5.0.2, diamond). EC/KO/GO/CAZy are computed annotations, not manual curation; cross-check against the primary literature before treating a specific reaction as established.

Conservation & selection (intra-MTBC, 145 209 strains)

pN/pS 0.34 · purifying
Polymorphic sites (≥ 0.1% of strains) 5 synonymous, 5 missense, 0 nonsense, 0 frameshift

pN/pS from segregating SNPs (singletons removed) normalised by possible sites. Low pN/pS = purifying selection (a strong signal that a "hypothetical" is a real, constrained gene). A high pN/pS is ambiguous: relaxed constraint or positive selection (drug resistance, antigenic variation) inflate it; e.g. rpoB/katG/pncA score high here for resistance, not loss of function. A clonal disruption (one allele over a clade) suggests lineage pseudogenisation; a convergent one (many independent alleles) is typical of resistance loss-of-function.

Domains (Pfam, hmmscan --cut_ga)

PfamAccessioni-EvalueResiduesDescription
Complex1_51KPF01512.23 2.2e-4454–229 Nuo51 FMN-binding domain
SLBBPF10531.16 2.0e-08255–299 SLBB domain
NADH_4Fe-4SPF10589.15 2.2e-33340–423 NADH-ubiquinone oxidoreductase-F iron-sulfur binding region

Functional interaction network (STRING v12, guilt-by-association)

Closest characterised functional partner: nuoD (NADH-quinone oxidoreductase subunit D), high confidence from genomic context alone (score 1000 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv3148 nuoD NADH-quinone oxidoreductase subunit D 999 1000 ctx neighborhood:881 coexpression:968 experimental:928 database:583 textmining:426
Rv3157 nuoM NADH-quinone oxidoreductase subunit M 999 1000 ctx neighborhood:760 coexpression:949 experimental:928 database:800 textmining:474
Rv3145 nuoA NADH-quinone oxidoreductase subunit A 999 1000 ctx neighborhood:879 coexpression:927 experimental:928 database:583 textmining:518
Rv3151 nuoG NADH-quinone oxidoreductase subunit G 999 1000 ctx neighborhood:881 cooccurence:759 coexpression:976 experimental:997 database:830 textmining:840
Rv3147 nuoC NADH-quinone oxidoreductase subunit C 999 1000 ctx neighborhood:881 coexpression:955 experimental:928 database:583 textmining:506
Rv3153 nuoI NADH-quinone oxidoreductase subunit I 999 1000 ctx neighborhood:700 cooccurence:620 coexpression:968 experimental:928 database:800 textmining:500
Rv3146 nuoB NADH-quinone oxidoreductase subunit B 999 1000 ctx neighborhood:881 coexpression:958 experimental:928 database:800
Rv3149 nuoE NADH-quinone oxidoreductase subunit E 999 1000 ctx neighborhood:881 fusion:675 cooccurence:774 coexpression:976 experimental:997 database:838 textmining:851
Rv3152 nuoH NADH-quinone oxidoreductase subunit H 999 1000 ctx neighborhood:725 coexpression:952 experimental:928 database:583 textmining:584
Rv3156 nuoL NADH-quinone oxidoreductase subunit L 999 999 ctx neighborhood:760 coexpression:953 experimental:911 textmining:589
Rv3154 nuoJ NADH-quinone oxidoreductase subunit J 999 999 ctx neighborhood:764 cooccurence:541 coexpression:953 experimental:911
Rv3158 nuoN NADH-quinone oxidoreductase subunit N 999 999 ctx neighborhood:760 coexpression:806 experimental:928 database:566 textmining:454
Rv3155 nuoK NADH-quinone oxidoreductase subunit K 998 998 ctx neighborhood:764 coexpression:876 experimental:911
Rv0310c hyp hypothetical protein 991 990 coexpression:722 experimental:928 database:561
Rv2782c pepR zinc protease 977 974 coexpression:701 experimental:917

STRING combines evidence channels (neighborhood, fusion, cooccurrence, coexpression, experimental, database, text-mining) into a 0–1000 score. The ctx badge marks edges carried by the genomic-context channels (conserved neighborhood, fusion, phylogenetic co-occurrence), which are independent of orthology and structure and the strongest signal for an unknown gene. The no text-mining column recomputes the score from data alone, so a link that does not depend on the literature is visible. Association is a function hypothesis, not proof: corroborate with the operon context and the primary literature before assigning a function.

Evidence

  • Legacy H37Rv annotation: NADH-quinone oxidoreductase subunit F
  • MTBC0 PGAP product: NADH-quinone oxidoreductase subunit NuoF
  • Pfam (hmmscan --cut_ga): Complex1_51K PF01512.23 (E=2e-44), SLBB PF10531.16 (E=2e-08), NADH_4Fe-4S PF10589.15 (E=2e-33)
  • (auto-curated by rules from PGAP + Pfam + Foldseek; not hand-reviewed)

Sources

  • Ancestral sequence & coordinates: Harrison LB et al. (2024), An imputed ancestral reference genome for the MTBC, doi:10.1101/2023.09.07.556366
  • Product annotation: NCBI PGAP on MTBC0; legacy from H37Rv NC_000962.3 (RefSeq NP_217666.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Complex1_51K (PF01512.23), SLBB (PF10531.16), NADH_4Fe-4S (PF10589.15)
  • Sequence-level signal: ESM Atlas (EvolutionaryScale × BioHub) — exploratory
  • Controlled vocabulary: eggNOG-mapper 2.1.12 (Cantalapiedra et al. 2021, doi:10.1093/molbev/msab293), eggNOG 5.0 DB (Huerta-Cepas et al. 2019) — OG COG1894
  • Curated reference: UniProt P9WIV7 (SwissProt, reviewed; Evidence at protein level)
  • Intra-MTBC selection: pN/pS and disruption from SPDI variants of 145 209 MTBC strains (this work, local collection vs H37Rv NC_000962.3)
  • Interaction network: STRING v12.0 (Szklarczyk et al. 2023, doi:10.1093/nar/gkac1000), taxon 83332, CC-BY 4.0 — 192 functional partner(s); context anchor nuoD
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_003348|Rv3150|nuoF
MTTQATPLTPVISRHWDDPESWTLATYQRHDRYRGYQALQKALTMPPDDVISIVKDSGLRGRGGAGFATGTKWSFIPQGDTGAAAKPHYLVVNADESEPGTCKDIPLMLATPHVLIEGVIIAAYAIRAHHAFVYVRGEVVPVLRRLHNAVAEAYAAGFLGRNIGGSGFDLELVVHAGAGAYICGEETALLDSLEGRRGQPRLRPPFPAVAGLYGCPTVINNVETIASVPSIILGGIDWFRSMGSEKSPGFTLYSLSGHVTRPGQYEAPLGITLRELLDYAGGVRAGHRLKFWTPGGSSTPLLTDEHLDVPLDYEGVGAAGSMLGTKALEIFDETTCVVRAVRRWTEFYKHESCGKCTPCREGTFWLDKIYERLETGRGSHEDIDKLLDISDSILGKSFCALGDGAASPVMSSIKHFRDEYLAHVEGGGCPFDPRDSMLVANGVDA