nuoH Family assigned · medium auto-curated
H37Rv Rv3152 · MTBC0 mtbc0_003350 ·
410 aa · 3541984–3543216 (+) ·
RefSeq NP_217668.1
Annotation: from legacy to revised
| Legacy (H37Rv / Mycobrowser) | NADH-quinone oxidoreductase subunit H |
|---|---|
| MTBC0 PGAP re-annotation | NADH-quinone oxidoreductase subunit NuoH |
| Revised (this work) | NADH-quinone oxidoreductase subunit NuoH. Pfam: NADHdh (PF00146.27). |
Auto-curated: this verdict and function were generated by rules from PGAP + Pfam + Foldseek and have not been hand-reviewed.
Curated reference (UniProt)
| UniProt |
P9WIX1
SwissProt · reviewed
· Evidence at protein level
|
|---|---|
| UniProt name | NADH-quinone oxidoreductase subunit H |
| 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 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 | nuoH |
| 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 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 | COG1005 |
| EC number |
EC 1.6.5.3
|
| KEGG orthology |
K00337
|
| 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 | 1.743 · diversifying/relaxed |
|---|---|
| Polymorphic sites (≥ 0.1% of strains) | 1 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)
| Pfam | Accession | i-Evalue | Residues | Description |
|---|---|---|---|---|
NADHdh | PF00146.27 | 2.9e-122 | 15–334 | NADH dehydrogenase |
Functional interaction network (STRING v12, guilt-by-association)
Closest characterised functional partner: nuoF (NADH-quinone oxidoreductase subunit F), high confidence from genomic context alone (score 1000 excluding text-mining).
| Partner | Product | Score | No text-mining | Channels (≥400) |
|---|---|---|---|---|
Rv3150 nuoF |
NADH-quinone oxidoreductase subunit F | 999 | 1000 ctx | neighborhood:725 coexpression:952 experimental:928 database:583 textmining:584 |
Rv3148 nuoD |
NADH-quinone oxidoreductase subunit D | 999 | 1000 ctx | neighborhood:724 cooccurence:772 coexpression:983 experimental:997 database:731 textmining:599 |
Rv3145 nuoA |
NADH-quinone oxidoreductase subunit A | 999 | 1000 ctx | neighborhood:762 cooccurence:774 coexpression:973 experimental:997 database:803 textmining:689 |
Rv3156 nuoL |
NADH-quinone oxidoreductase subunit L | 999 | 1000 ctx | neighborhood:874 cooccurence:774 coexpression:976 experimental:922 textmining:810 |
Rv3157 nuoM |
NADH-quinone oxidoreductase subunit M | 999 | 1000 ctx | neighborhood:874 cooccurence:773 coexpression:974 experimental:928 database:803 textmining:853 |
Rv3149 nuoE |
NADH-quinone oxidoreductase subunit E | 999 | 1000 ctx | neighborhood:727 coexpression:963 experimental:928 database:620 textmining:590 |
Rv3146 nuoB |
NADH-quinone oxidoreductase subunit B | 999 | 1000 ctx | neighborhood:721 cooccurence:770 coexpression:980 experimental:997 database:731 |
Rv3153 nuoI |
NADH-quinone oxidoreductase subunit I | 999 | 1000 ctx | neighborhood:881 fusion:633 cooccurence:758 coexpression:976 experimental:997 database:731 textmining:744 |
Rv3147 nuoC |
NADH-quinone oxidoreductase subunit C | 999 | 1000 ctx | neighborhood:722 cooccurence:769 coexpression:955 experimental:997 database:731 textmining:686 |
Rv3158 nuoN |
NADH-quinone oxidoreductase subunit N | 999 | 1000 ctx | neighborhood:874 cooccurence:773 coexpression:970 experimental:928 database:747 textmining:735 |
Rv3154 nuoJ |
NADH-quinone oxidoreductase subunit J | 999 | 1000 ctx | neighborhood:881 cooccurence:751 coexpression:976 experimental:997 textmining:688 |
Rv3151 nuoG |
NADH-quinone oxidoreductase subunit G | 999 | 1000 ctx | neighborhood:764 coexpression:965 experimental:928 database:583 |
Rv3155 nuoK |
NADH-quinone oxidoreductase subunit K | 999 | 1000 ctx | neighborhood:881 cooccurence:773 coexpression:957 experimental:924 textmining:625 |
Rv2196 qcrB |
ubiquinol-cytochrome C reductase cytochrome subunit B | 987 | 984 | coexpression:855 experimental:894 |
Rv2193 ctaE |
cytochrome C oxidase subunit III | 981 | 976 | coexpression:859 experimental:794 |
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 H
- MTBC0 PGAP product: NADH-quinone oxidoreductase subunit NuoH
- Pfam (hmmscan --cut_ga): NADHdh PF00146.27 (E=3e-122)
- (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_217668.1)
- Domains: Pfam-A via hmmscan --cut_ga — NADHdh (PF00146.27)
- 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
COG1005 - Curated reference: UniProt P9WIX1 (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 —
140 functional partner(s); context anchor
nuoF - Primary literature: none located yet; annotation rests on the domain/homology sources above.
Ancestral MTBC0 protein sequence
>mtbc0_003350|Rv3152|nuoH MTTFGHDTWWLVAAKAIAVFVFLMLTVLVAILAERKLLGRMQLRPGPNRVGPKGALQSLADGIKLALKESITPGGIDRFVYFVAPIISVIPAFTAFAFIPFGPEVSVFGHRTPLQITDLPVAVLFILGLSAIGVYGIVLGGWASGSTYPLLGGVRSTAQVISYEVAMGLSFATVFLMAGTMSTSQIVAAQDGVWYAFLLLPSFVIYLISMVGETNRAPFDLPEAEGELVAGFHTEYSSLKFAMFMLAEYVNMTTVSALAATLFFGGWHAPWPLNMWASANTGWWPLIWFTAKVWGFLFIYFWLRATLPRLRYDQFMALGWKLLIPVSLVWVMVAAIIRSLRNQGYQYWTPTLVFSSIVVAAAMVLLLRKPLSAPGARASARQRGDEGTSPEPAFPTPPLLAGATKENAGG