mqo Resolved · high auto-curated
H37Rv Rv2852c · MTBC0 mtbc0_003031 ·
493 aa · 3181246–3182727 (-) ·
RefSeq NP_217368.1
Annotation: from legacy to revised
| Legacy (H37Rv / Mycobrowser) | malate:quinone oxidoreductase |
|---|---|
| MTBC0 PGAP re-annotation | malate dehydrogenase (quinone) |
| Revised (this work) | Malate dehydrogenase (quinone). Pfam: Mqo (PF06039.22), DAO (PF01266.31). |
Auto-curated: this verdict and function were generated by rules from PGAP + Pfam + Foldseek and have not been hand-reviewed.
Curated reference (UniProt)
| UniProt |
P9WJP5
SwissProt · reviewed
· Evidence at protein level
|
|---|---|
| UniProt name | Probable malate:quinone oxidoreductase |
| EC (curated) |
EC 1.1.5.4
|
Functional vocabulary (eggNOG-mapper, orthology transfer)
| COG category |
C Energy production and conversion
|
|---|---|
| Preferred name | mqo |
| eggNOG description | malate quinone oxidoreductase |
| Orthologous group | COG0579 |
| EC number |
EC 1.1.5.4
|
| KEGG orthology |
K00116
|
| KEGG pathways |
map00020, map00620, map01100, map01110, map01120, map01130, map01200
|
| KEGG modules |
M00009, M00011
|
| Gene Ontology (15) |
GO:0003674, GO:0003824, GO:0005575, GO:0005622, GO:0005623, GO:0005737, GO:0005886, GO:0008150, GO:0008152, GO:0016020, GO:0016491, GO:0044424 +3 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 | 0.567 · relaxed/neutral |
|---|---|
| Polymorphic sites (≥ 0.1% of strains) | 3 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 |
|---|---|---|---|---|
Mqo | PF06039.22 | 8.6e-211 | 6–490 | Malate:quinone oxidoreductase (Mqo) |
DAO | PF01266.31 | 2.4e-12 | 8–249 | FAD dependent oxidoreductase |
Functional interaction network (STRING v12, guilt-by-association)
Closest characterised functional partner: Rv2851c (GCN5-like N-acetyltransferase), high confidence from genomic context alone (score 814 excluding text-mining).
| Partner | Product | Score | No text-mining | Channels (≥400) |
|---|---|---|---|---|
Rv1131 prpC |
methylcitrate synthase PrpC | 974 | 941 | coexpression:412 database:900 textmining:590 |
Rv0896 gltA2 |
citrate synthase 1 | 969 | 941 | coexpression:416 database:900 textmining:508 |
Rv0889c citA |
citrate synthase 2 | 946 | 941 | coexpression:417 database:900 |
Rv1240 mdh |
malate dehydrogenase | 962 | 913 | database:900 textmining:586 |
Rv2967c pca |
pyruvate carboxylase | 935 | 913 | database:900 |
Rv1098c fum |
fumarate hydratase | 970 | 905 | database:900 textmining:707 |
Rv2332 mez |
malate oxidoreductase | 917 | 904 | database:900 |
Rv1837c glcB |
malate synthase | 972 | 903 | database:900 textmining:729 |
Rv0211 pckA |
phosphoenolpyruvate carboxykinase | 925 | 903 | database:900 |
Rv3859c gltB |
glutamate synthase large subunit | 914 | 851 | database:800 textmining:452 |
Rv0234c gabD1 |
succinate-semialdehyde dehydrogenase | 851 | 843 | database:800 |
Rv1731 gabD2 |
succinate-semialdehyde dehydrogenase | 850 | 842 | database:800 |
Rv2964 purU |
formyltetrahydrofolate deformylase | 819 | 820 | database:800 |
Rv2851c |
GCN5-like N-acetyltransferase | 841 | 814 ctx | neighborhood:804 |
Rv1659 argH |
argininosuccinate lyase | 829 | 812 | database:800 |
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: malate:quinone oxidoreductase
- MTBC0 PGAP product: malate dehydrogenase (quinone)
- Pfam (hmmscan --cut_ga): Mqo PF06039.22 (E=9e-211), DAO PF01266.31 (E=2e-12)
- (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_217368.1)
- Domains: Pfam-A via hmmscan --cut_ga — Mqo (PF06039.22), DAO (PF01266.31)
- 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
COG0579 - Curated reference: UniProt P9WJP5 (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 —
48 functional partner(s); context anchor
Rv2851c - Primary literature: none located yet; annotation rests on the domain/homology sources above.
Ancestral MTBC0 protein sequence
>mtbc0_003031|Rv2852c|mqo MSDLARTDVVLIGAGIMSATLGVLLRRLEPNWSITLIERLDAVAAESSGPWNNAGTGHSALCEMNYTPEMPDGSIDITKAVRVNEQFQVTRQFWAYAAENGILTDVRSFLNPVPHVSFVHGSRGVEYLRRRQKALAGNPLFAGTEFIESPDEFARRLPFMAAKRAFSEPVALNWAADGTDVDFGALAKQLIGYCVQNGTTALFGHEVRNLSRQSDGSWTVTMCNRRTGEKRKLNTKFVFVGAGGDTLPVLQKSGIKEVKGFAGFPIGGRFLRAGNPALTASHRAKVYGFPAPGAPPLGALHLDLRFVNGKSWLVFGPYAGWSPKFLKHGQISDLPRSIRPDNLLSVLGVGLTERRLLNYLISQLRLSEPERVSALREFAPSAIDSDWELTIAGQRVQVIRRDERNGGVLEFGTTVIGDADGSIAGLLGGSPGASTAVAIMLDVLQKCFANRYQSWLPTLKEMVPSLGVQLSNEPALFDEVWSWSTKALKLGAA