nuoB Family assigned · medium auto-curated
H37Rv Rv3146 · MTBC0 - ·
184 aa · 3512077–3512631 (+) ·
RefSeq NP_217662.1
Annotation: from legacy to revised
| Legacy (H37Rv / Mycobrowser) | NADH-quinone oxidoreductase subunit B |
|---|---|
| MTBC0 PGAP re-annotation | — |
| Revised (this work) | NADH-quinone oxidoreductase subunit B. Pfam: Oxidored_q6 (PF01058.30). |
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 |
P9WJH1
SwissProt · reviewed
· Evidence at protein level
|
|---|---|
| UniProt name | NADH-quinone oxidoreductase subunit B |
| EC (curated) |
EC 7.1.1.-
|
| Curated function | NDH-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 a 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. |
Functional vocabulary (eggNOG-mapper, orthology transfer)
| COG category |
C Energy production and conversion
|
|---|---|
| Preferred name | nuoB |
| eggNOG description | NDH-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 a 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 |
| Orthologous group | COG0377 |
| EC number |
EC 1.6.5.3
|
| KEGG orthology |
K00331
|
| 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 | 0.0 · strong purifying |
|---|---|
| Polymorphic sites (≥ 0.1% of strains) | 2 synonymous, 0 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)
| Pfam | Accession | i-Evalue | Residues | Description |
|---|---|---|---|---|
Oxidored_q6 | PF01058.30 | 5.4e-30 | 37–146 | NADH ubiquinone oxidoreductase, 20 Kd subunit |
Functional interaction network (STRING v12, guilt-by-association)
Closest characterised functional partner: nuoK (NADH-quinone oxidoreductase subunit K), high confidence from genomic context alone (score 1000 excluding text-mining).
| Partner | Product | Score | No text-mining | Channels (≥400) |
|---|---|---|---|---|
Rv3155 nuoK |
NADH-quinone oxidoreductase subunit K | 999 | 1000 ctx | neighborhood:764 cooccurence:760 coexpression:979 experimental:924 |
Rv3151 nuoG |
NADH-quinone oxidoreductase subunit G | 999 | 1000 ctx | neighborhood:881 coexpression:958 experimental:997 database:895 textmining:448 |
Rv3154 nuoJ |
NADH-quinone oxidoreductase subunit J | 999 | 1000 ctx | neighborhood:764 cooccurence:682 coexpression:937 experimental:997 |
Rv3158 nuoN |
NADH-quinone oxidoreductase subunit N | 999 | 1000 ctx | neighborhood:760 cooccurence:757 coexpression:948 experimental:928 database:666 textmining:714 |
Rv3147 nuoC |
NADH-quinone oxidoreductase subunit C | 999 | 1000 ctx | neighborhood:882 cooccurence:761 coexpression:958 experimental:997 database:844 |
Rv3149 nuoE |
NADH-quinone oxidoreductase subunit E | 999 | 1000 ctx | neighborhood:882 coexpression:968 experimental:928 database:800 textmining:564 |
Rv3153 nuoI |
NADH-quinone oxidoreductase subunit I | 999 | 1000 ctx | neighborhood:686 cooccurence:771 coexpression:979 experimental:997 database:925 |
Rv3152 nuoH |
NADH-quinone oxidoreductase subunit H | 999 | 1000 ctx | neighborhood:721 cooccurence:770 coexpression:980 experimental:997 database:731 |
Rv3156 nuoL |
NADH-quinone oxidoreductase subunit L | 999 | 1000 ctx | neighborhood:760 cooccurence:754 coexpression:937 experimental:922 |
Rv3157 nuoM |
NADH-quinone oxidoreductase subunit M | 999 | 1000 ctx | neighborhood:760 cooccurence:744 coexpression:941 experimental:928 database:871 |
Rv3145 nuoA |
NADH-quinone oxidoreductase subunit A | 999 | 1000 ctx | neighborhood:879 cooccurence:762 coexpression:973 experimental:997 database:731 textmining:630 |
Rv3148 nuoD |
NADH-quinone oxidoreductase subunit D | 999 | 1000 ctx | neighborhood:882 fusion:900 cooccurence:774 coexpression:979 experimental:997 database:844 textmining:509 |
Rv3150 nuoF |
NADH-quinone oxidoreductase subunit F | 999 | 1000 ctx | neighborhood:881 coexpression:958 experimental:928 database:800 |
Rv3143 |
response regulator | 998 | 998 ctx | neighborhood:473 experimental:997 |
Rv0310c hyp |
hypothetical protein | 994 | 994 | coexpression:507 experimental:928 database:844 |
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): NADH-quinone oxidoreductase subunit B
- Pfam (hmmscan --cut_ga): Oxidored_q6 PF01058.30 (E=5e-30)
- (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_217662.1)
- Domains: Pfam-A via hmmscan --cut_ga — Oxidored_q6 (PF01058.30)
- 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
COG0377 - Curated reference: UniProt P9WJH1 (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 —
165 functional partner(s); context anchor
nuoK - Primary literature: none located yet; annotation rests on the domain/homology sources above.
Ancestral MTBC0 protein sequence
>H37Rv|Rv3146|nuoB MGLEEQLPGGILLSTVEKVAGYVRKNSLWPATFGLACCAIEMMATAGPRFDIARFGMERFSATPRQADLMIVAGRVSQKMAPVLRQIYDQMAEPKWVLAMGVCASSGGMFNNYAIVQGVDHVVPVDIYLPGCPPRPEMLLHAILKLHEKIQQMPLGINRERAIAEAEEAALLARPTIEMRGLLR