mez Resolved · high auto-curated

H37Rv Rv2332 · MTBC0 mtbc0_002482 · 548 aa · 2629857–2631503 (+) · RefSeq NP_216848.2

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)malate oxidoreductase
MTBC0 PGAP re-annotationNAD-dependent malic enzyme
Revised (this work)NAD-dependent malic enzyme. Pfam: malic (PF00390.25), Malic_M (PF03949.22).

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

Curated reference (UniProt)

UniProt P9WK25 SwissProt · reviewed · Evidence at protein level
UniProt namePutative malate oxidoreductase [NAD]
EC (curated) EC 1.1.1.38

UniProt still lists this protein as Putative malate oxidoreductase [NAD]; the revised annotation above is ahead of the current UniProt record.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category C Energy production and conversion
Preferred namemez
eggNOG descriptionmalic enzyme
Orthologous groupCOG0281
EC number EC 1.1.1.38, EC 4.1.1.101
KEGG orthology K00027, K22212
KEGG pathways map00620, map01120, map01200, map02020
Gene Ontology (28) GO:0003674, GO:0003824, GO:0004470, GO:0005575, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0006082, GO:0006090, GO:0006108, GO:0008150 +16 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 0.544 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 5 synonymous, 8 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
malicPF00390.25 4.0e-6674–254 Malic enzyme, N-terminal domain
Malic_MPF03949.22 6.9e-100265–522 Malic enzyme, NAD binding domain

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

PartnerProductScoreNo text-miningChannels (≥400)
Rv1240 mdh malate dehydrogenase 978 947 database:900 textmining:605
Rv1098c fum fumarate hydratase 975 945 coexpression:418 database:900 textmining:567
Rv1617 pykA pyruvate kinase 975 939 database:900 textmining:623
Rv2496c bkdB 3-methyl-2-oxobutanoate dehydrogenase subunit beta 947 925 database:900
Rv2967c pca pyruvate carboxylase 987 919 database:900 textmining:848
Rv1837c glcB malate synthase 940 907 database:900
Rv2241 aceE pyruvate dehydrogenase E1 component 937 907 database:900
Rv2497c bkdA 3-methyl-2-oxobutanoate dehydrogenase subunit alpha 932 907 database:900
Rv1127c ppdK pyruvate, phosphate dikinase PpdK 917 906 database:900
Rv2455c korA 2-oxoglutarate oxidoreductase subunit KorA 961 905 database:900 textmining:615
Rv2852c mqo malate:quinone oxidoreductase 917 904 database:900
Rv1872c lldD2 L-lactate dehydrogenase 915 903 database:900
Rv0694 mftD mycofactocin system heme/flavin oxidoreductase MftD 912 903 database:900
Rv2454c korB 2-oxoglutarate oxidoreductase subunit KorB 935 900 database:900
Rv3509c ilvX acetohydroxyacid synthase large subunit 854 844 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 oxidoreductase
  • MTBC0 PGAP product: NAD-dependent malic enzyme
  • Pfam (hmmscan --cut_ga): malic PF00390.25 (E=4e-66), Malic_M PF03949.22 (E=7e-100)
  • (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_216848.2)
  • Domains: Pfam-A via hmmscan --cut_ga — malic (PF00390.25), Malic_M (PF03949.22)
  • 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 COG0281
  • Curated reference: UniProt P9WK25 (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 — 105 functional partner(s)
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_002482|Rv2332|mez
MSDARVPRIPAALSAPSLNRGVGFTHAQRRRLGLTGRLPSAVLTLDQQAERVWHQLQSLATDLGRNLLLEQLHYRHEVLYFKVLADHLPELMPVVYTPTVGEAIQRFSDEYRGQRGLFLSIDEPDEIEEAFNTLGLGPEDVDLIVCTDAEAILGIGDWGVGGIQIAVGKLALYTAGGGVDPRRCLAVSLDVGTDNEQLLADPFYLGNRHARRRGREYDEFVSRYIETAQRLFPRAILHFEDFGPANARKILDTYGTDYCVFNDDMQGTGAVVLAAVYSGLKVTGIPLRDQTIVVFGAGTAGMGIADQIRDAMVADGATLEQAVSQIWPIDRPGLLFDDMDDLRDFQVPYAKNRHQLGVAVGDRVGLSDAIKIASPTILLGCSTVYGAFTKEVVEAMTASCKHPMIFPLSNPTSRMEAIPADVLAWSNGRALLATGSPVAPVEFDETTYVIGQANNVLAFPGIGLGVIVAGARLITRRMLHAAAKAIAHQANPTNPGDSLLPDVQNLRAISTTVAEAVYRAAVQDGVASRTHDDVRQAIVDTMWLPAYD