nuoG Family assigned · medium auto-curated

H37Rv Rv3151 · MTBC0 mtbc0_003349 · 806 aa · 3539448–3541868 (+) · RefSeq NP_217667.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)NADH-quinone oxidoreductase subunit G
MTBC0 PGAP re-annotationNADH-quinone oxidoreductase subunit G
Revised (this work)NADH-quinone oxidoreductase subunit G. Pfam: Fer2_4 (PF13510.12), Fer2 (PF00111.33), NADH-G_4Fe-4S_3 (PF10588.15), Fer4_Nqo3 (PF22117.3), Molybdopterin (PF00384.28), Molydop_binding (PF01568.28).

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

Curated reference (UniProt)

UniProt P9WIV9 SwissProt · reviewed · Evidence at protein level
UniProt nameNADH-quinone oxidoreductase subunit G
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)..; FUNCTION: Plays a critical role in M.tuberculosis ability to inhibit apoptosis of infected macrophages; thus helps the bacterium in its struggle to resist th.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category C Energy production and conversion
Preferred namenuoG
eggNOG descriptionNADH-quinone oxidoreductase
Orthologous groupCOG1034
EC number EC 1.6.5.3
KEGG orthology K00336
KEGG pathways map00190, map01100
KEGG modules M00144
Gene Ontology (48) GO:0003674, GO:0003824, GO:0003954, GO:0005488, GO:0005575, GO:0005618, GO:0005623, GO:0005886, GO:0008150, GO:0008152, GO:0009405, GO:0010941 +36 more

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 0.304 · purifying
Polymorphic sites (≥ 0.1% of strains) 13 synonymous, 11 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
Fer2_4PF13510.12 3.8e-2015–90 2Fe-2S iron-sulfur cluster binding domain
Fer2PF00111.33 7.1e-0621–81 2Fe-2S iron-sulfur cluster binding domain
NADH-G_4Fe-4S_3PF10588.15 1.8e-15101–139 NADH-ubiquinone oxidoreductase-G iron-sulfur binding region
Fer4_Nqo3PF22117.3 3.3e-20157–220 NADH-quinone oxidoreductase subunit 3, ferredoxin-like domain
MolybdopterinPF00384.28 2.3e-20291–639 Molybdopterin oxidoreductase
Molydop_bindingPF01568.28 4.8e-09730–785 Molydopterin dinucleotide binding domain

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 cooccurence:574 coexpression:968 experimental:997 database:781
Rv3150 nuoF NADH-quinone oxidoreductase subunit F 999 1000 ctx neighborhood:881 cooccurence:759 coexpression:976 experimental:997 database:830 textmining:840
Rv3157 nuoM NADH-quinone oxidoreductase subunit M 999 1000 ctx neighborhood:760 coexpression:970 experimental:928 database:800 textmining:450
Rv3145 nuoA NADH-quinone oxidoreductase subunit A 999 1000 ctx neighborhood:879 coexpression:884 experimental:928 database:583 textmining:662
Rv3158 nuoN NADH-quinone oxidoreductase subunit N 999 1000 ctx neighborhood:760 coexpression:953 experimental:928 database:566 textmining:804
Rv3147 nuoC NADH-quinone oxidoreductase subunit C 999 1000 ctx neighborhood:881 cooccurence:741 coexpression:966 experimental:997 database:781
Rv3154 nuoJ NADH-quinone oxidoreductase subunit J 999 1000 ctx neighborhood:764 cooccurence:745 coexpression:962 experimental:911
Rv3152 nuoH NADH-quinone oxidoreductase subunit H 999 1000 ctx neighborhood:764 coexpression:965 experimental:928 database:583
Rv3153 nuoI NADH-quinone oxidoreductase subunit I 999 1000 ctx neighborhood:764 cooccurence:744 coexpression:974 experimental:997 database:895
Rv3146 nuoB NADH-quinone oxidoreductase subunit B 999 1000 ctx neighborhood:881 coexpression:958 experimental:997 database:895 textmining:448
Rv3149 nuoE NADH-quinone oxidoreductase subunit E 999 1000 ctx neighborhood:881 cooccurence:770 coexpression:976 experimental:997 database:838 textmining:774
Rv3156 nuoL NADH-quinone oxidoreductase subunit L 999 999 ctx neighborhood:760 coexpression:964 experimental:911 textmining:591
Rv3143 response regulator 999 999 ctx cooccurence:740 experimental:997
Rv3155 nuoK NADH-quinone oxidoreductase subunit K 999 998 ctx neighborhood:764 coexpression:859 experimental:911 textmining:630
Rv0310c hyp hypothetical protein 993 992 coexpression:634 experimental:928 database:738

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 G
  • MTBC0 PGAP product: NADH-quinone oxidoreductase subunit G
  • Pfam (hmmscan --cut_ga): Fer2_4 PF13510.12 (E=4e-20), Fer2 PF00111.33 (E=7e-06), NADH-G_4Fe-4S_3 PF10588.15 (E=2e-15), Fer4_Nqo3 PF22117.3 (E=3e-20), Molybdopterin PF00384.28 (E=2e-20), Molydop_binding PF01568.28 (E=5e-09)
  • (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_217667.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Fer2_4 (PF13510.12), Fer2 (PF00111.33), NADH-G_4Fe-4S_3 (PF10588.15), Fer4_Nqo3 (PF22117.3), Molybdopterin (PF00384.28), Molydop_binding (PF01568.28)
  • 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 COG1034
  • Curated reference: UniProt P9WIV9 (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 — 191 functional partner(s); context anchor nuoD
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_003349|Rv3151|nuoG
MTQAADTDIRVGQPEMVTLTIDGVEISVPKGTLVIRAAELMGIQIPRFCDHPLLEPVGACRQCLVEVEGQRKPLASCTTVATDDMVVRTQLTSEIADKAQHGVMELLLINHPLDCPMCDKGGECPLQNQAMSNGRTDSRFTEAKRTFAKPINISAQVLLDRERCILCARCTRFSDQIAGDPFIDMQERGALQQVGIYADEPFESYFSGNTVQICPVGALTGTAYRFRARPFDLVSSPSVCEHCASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDVITTPLIRDGGDPKGALVPTSWSHAMAVAAQGLAAARGRTGVLVGGRVTWEDAYAYAKFARITLGTNDIDFRARPHSAEEADFLAARIAGRHMAVSYADLESAPVVLLVGFEPEDESPIVFLRLRKAARRHRVPVYTIAPFATGGLHKMSGRLIKTVPGGEPAALDDLATGAVGDLLATPGAVIMVGERLATVPGGLSAAARLADTTGARLAWVPRRAGERGALEAGALPTLLPGGRPLADEVARAQVCAAWHIAELPAAAGRDADGILAAAADETLAALLVGGIEPADFADPDAVLAALDATGFVVSLELRHSAVTERADVVFPVAPTTQKAGAFVNWEGRYRTFEPALRGSTLQAGQSDHRVLDALADDMGVHLGVPTVEAAREELAALGIWDGKHAAGPHIAATGPTQPEAGEAILTGWRMLLDEGRLQDGEPYLAGTARTPVVRLSPDTAAEIGAADGEAVTVSTSRGSITLPCSVTDMPDRVVWLPLNSAGSTVHRQLRVTIGSIVKIGAGS