mmsB Resolved · high auto-curated

H37Rv Rv0751c · MTBC0 mtbc0_000798 · 294 aa · 846772–847656 (-) · RefSeq NP_215265.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)3-hydroxyisobutyrate dehydrogenase
MTBC0 PGAP re-annotation3-hydroxyisobutyrate dehydrogenase
Revised (this work)3-hydroxyisobutyrate dehydrogenase. Pfam: NAD_binding_2 (PF03446.22), F420_oxidored (PF03807.24), 2-Hacid_dh_C (PF02826.26), NAD_binding_11 (PF14833.12).

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

Curated reference (UniProt)

UniProt P9WNY5 SwissProt · reviewed · Evidence at protein level
UniProt nameProbable 3-hydroxyisobutyrate dehydrogenase
EC (curated) EC 1.1.1.31

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Preferred namemmsB
eggNOG descriptionBelongs to the 3-hydroxyisobutyrate dehydrogenase family
Orthologous groupCOG2084
EC number EC 1.1.1.31
KEGG orthology K00020
KEGG pathways map00280, map01100

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 1.08 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 2 synonymous, 6 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
NAD_binding_2PF03446.22 2.3e-453–159 NAD binding domain of 6-phosphogluconate dehydrogenase
F420_oxidoredPF03807.24 2.7e-073–69 NADP oxidoreductase coenzyme F420-dependent
2-Hacid_dh_CPF02826.26 1.2e-053–104 D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain
NAD_binding_11PF14833.12 1.6e-32162–287 NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase

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

Closest characterised functional partner: mmsA (methylmalonate-semialdehyde dehydrogenase), high confidence from genomic context alone (score 998 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0753c mmsA methylmalonate-semialdehyde dehydrogenase 998 998 ctx neighborhood:875 cooccurence:426 coexpression:753 database:900
Rv0752c fadE9 acyl-CoA dehydrogenase FadE9 988 989 ctx neighborhood:879 cooccurence:516 coexpression:821
Rv1071c echA9 enoyl-CoA hydratase EchA9 965 963 ctx fusion:898 cooccurence:474
Rv0860 fadB fatty oxidation protein FadB 946 921 database:900
Rv0147 aldehyde dehydrogenase 916 912 database:900
Rv0768 aldA aldehyde dehydrogenase AldA 916 912 database:900
Rv3293 pcd piperideine-6-carboxylic acid dehydrogenase 915 912 database:900
Rv0223c aldehyde dehydrogenase 915 912 database:900
Rv2589 gabT 4-aminobutyrate aminotransferase 900 901 database:900
Rv2501c accA1 acetyl/propionyl-CoA carboxylase subuit alpha 837 834 database:800
Rv0973c accA2 acetyl/propionyl-CoA carboxylase subuit alpha 836 832 database:800
Rv3285 accA3 bifunctional protein acetyl-/propionyl-CoA carboxylase subunit alpha AccA 835 832 database:800
Rv3667 acs acetyl-CoAsynthetase 824 817 database:800
Rv3280 accD5 propionyl-CoA carboxylase subunit beta 807 807 database:800
Rv2247 accD6 acetyl-/propionyl-CoA carboxylase subunit beta 807 807 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: 3-hydroxyisobutyrate dehydrogenase
  • MTBC0 PGAP product: 3-hydroxyisobutyrate dehydrogenase
  • Pfam (hmmscan --cut_ga): NAD_binding_2 PF03446.22 (E=2e-45), F420_oxidored PF03807.24 (E=3e-07), 2-Hacid_dh_C PF02826.26 (E=1e-05), NAD_binding_11 PF14833.12 (E=2e-32)
  • (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_215265.1)
  • Domains: Pfam-A via hmmscan --cut_ga — NAD_binding_2 (PF03446.22), F420_oxidored (PF03807.24), 2-Hacid_dh_C (PF02826.26), NAD_binding_11 (PF14833.12)
  • 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 COG2084
  • Curated reference: UniProt P9WNY5 (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 — 25 functional partner(s); context anchor mmsA
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_000798|Rv0751c|mmsB
MTTIAFLGLGNMGAPMSANLVGAGHVVRGFDPAPTAASGAAAHGVAVFRSAPEAVAEADVVITMLPTGEVVRRCYTDVLAAARPATLFIDSSTISVTDAREVHALAESHGMLQLDAPVSGGVKGAAAATLAFMVGGDESTLRRARPVLEPMAGKIIHCGAAGAGQAAKVCNNMVLAVQQIAIAEAFVLAEKLGLSAQSLFDVITGATGNCWAVHTNCPVPGPVPTSPANNDFKPGFSTALMNKDLGLAMDAVAATGATAPLGSHAADIYAKFAADHADLDFSAVIHTLRARADA