Rv3178 Resolved · high auto-curated

H37Rv Rv3178 · MTBC0 - · 119 aa · 3546438–3546797 (+) · RefSeq NP_217694.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)nitroreductase
MTBC0 PGAP re-annotation
Revised (this work)Nitroreductase. Pfam: F420H2_quin_red (PF04075.21).

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

Annotated on the H37Rv protein: this gene has no 1:1 ancestral MTBC0 anchor (PE/PPE, paralogue, IS element, or otherwise unanchored CDS).

Curated reference (UniProt)

UniProt O53328 SwissProt · reviewed · Inferred from homology
UniProt namePutative F420H(2)-dependent quinone reductase Rv3178
EC (curated) EC 1.1.98.-
Curated functionInvolved in a F420-dependent anti-oxidant mechanism that protects M.tuberculosis against oxidative stress and bactericidal agents. Catalyzes the F420H(2)-dependent two-electron reduction of quinones to dihydroquinones, thereby preventing the formation of cytotoxic semiquinones obtained by the one-electron reduction pathway. Since menaquinone is the sole quinone electron carrier in the respiratory chain in M.tuberculosis, the physiological electron acceptor for Fqr-mediated F420H(2) oxidation is therefore likely to be the endogenous menaquinone found in the membrane fraction of M.tuberculosis.

UniProt still lists this protein as Putative F420H(2)-dependent quinone reductase Rv3178; the revised annotation above is ahead of the current UniProt record.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category P Inorganic ion transport and metabolism
eggNOG descriptionF420H(2)-dependent quinone reductase
Orthologous groupCOG0748
Gene Ontology (24) GO:0003674, GO:0005488, GO:0005575, GO:0005618, GO:0005623, GO:0005886, GO:0008150, GO:0008152, GO:0016020, GO:0030312, GO:0031406, GO:0036094 +12 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 1.035 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 1 synonymous, 3 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
F420H2_quin_redPF04075.21 1.6e-2911–117 F420H(2)-dependent quinone reductase

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

Closest characterised functional partner: Rv0044c (oxidoreductase), high confidence from genomic context alone (score 760 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0044c oxidoreductase 774 760 ctx cooccurence:759
Rv3520c coenzyme F420-dependent oxidoreductase 773 760 ctx cooccurence:758
Rv3261 fbiA 2-phospho-L-lactate transferase 869 753 ctx cooccurence:746 textmining:493
Rv0407 fgd1 F420-dependent glucose-6-phosphate dehydrogenase 953 745 ctx cooccurence:745 textmining:824
Rv1855c oxidoreductase 749 734 ctx cooccurence:732
Rv2951c phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase 740 724 ctx cooccurence:724
Rv3262 fbiB coenzyme F420:L-glutamate ligase 836 717 ctx cooccurence:707 textmining:446
Rv0132c fgd2 F420-dependent glucose-6-phosphate dehydrogenase 731 715 ctx cooccurence:712
Rv2983 cofC 2-phospho-L-lactate guanylyltransferase 740 709 ctx cooccurence:700
Rv3093c oxidoreductase 702 684 ctx cooccurence:684
Rv0940c oxidoreductase 685 665 ctx cooccurence:663
Rv2161c hyp hypothetical protein 676 656 ctx cooccurence:653
Rv3177 peroxidase 651 652 ctx neighborhood:526
Rv0791c hyp hypothetical protein 670 649 ctx cooccurence:647
Rv3072c hyp hypothetical protein 659 638 ctx cooccurence:638

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

  • Annotation from H37Rv (no MTBC0 1:1 anchor; H37Rv protein used): nitroreductase
  • Pfam (hmmscan --cut_ga): F420H2_quin_red PF04075.21 (E=2e-29)
  • (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_217694.1)
  • Domains: Pfam-A via hmmscan --cut_ga — F420H2_quin_red (PF04075.21)
  • 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 COG0748
  • Curated reference: UniProt O53328 (SwissProt, reviewed; Inferred from homology)
  • 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 — 34 functional partner(s); context anchor Rv0044c
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>H37Rv|Rv3178|
MRLGAGFRKPVPTLLLEHRSRKSGKNFVAPLLYITDRNNVIVVASALGQAENPQWYRNLPPNPDTHIQIGSDRRPVRAVVASSDERARLWPRPVDAYADFDSCQSWTERGIPVIILRPR