leuC Family assigned · medium auto-curated

H37Rv Rv2988c · MTBC0 mtbc0_003173 · 473 aa · 3365963–3367384 (-) · RefSeq NP_217504.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)3-isopropylmalate dehydratase large subunit
MTBC0 PGAP re-annotation3-isopropylmalate dehydratase large subunit
Revised (this work)3-isopropylmalate dehydratase large subunit. Pfam: Aconitase (PF00330.26).

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

Curated reference (UniProt)

UniProt P9WQF5 SwissProt · reviewed · Evidence at protein level
UniProt name3-isopropylmalate dehydratase large subunit
EC (curated) EC 4.2.1.33
Curated functionCatalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category E Amino acid transport and metabolism
Preferred nameleuC
eggNOG descriptionCatalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate
Orthologous groupCOG0065
EC number EC 4.2.1.33, EC 4.2.1.35
KEGG orthology K01703
KEGG pathways map00290, map00660, map00966, map01100, map01110, map01210, map01230
KEGG modules M00432, M00535
Gene Ontology (6) GO:0005575, GO:0005618, GO:0005623, GO:0030312, GO:0044464, GO:0071944

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 0.23 · purifying
Polymorphic sites (≥ 0.1% of strains) 6 synonymous, 4 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
AconitasePF00330.26 5.8e-17713–464 Aconitase family (aconitate hydratase)

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

Closest characterised functional partner: leuD (3-isopropylmalate dehydratase small subunit), high confidence from genomic context alone (score 1000 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv2987c leuD 3-isopropylmalate dehydratase small subunit 999 1000 ctx neighborhood:849 fusion:899 cooccurence:774 coexpression:976 experimental:511 database:900 textmining:948
Rv2995c leuB 3-isopropylmalate dehydrogenase 999 997 ctx cooccurence:695 coexpression:857 database:900 textmining:702
Rv3710 leuA 2-isopropylmalate synthase 990 976 coexpression:696 database:900 textmining:615
Rv2989 transcriptional regulator 983 969 ctx neighborhood:785 coexpression:860 textmining:499
Rv0189c ilvD dihydroxy-acid dehydratase 967 933 ctx cooccurence:546 coexpression:846 textmining:540
Rv3001c ilvC ketol-acid reductoisomerase 958 903 coexpression:852 textmining:588
Rv3002c ilvN acetolactate synthase small subunit 867 828 coexpression:777
Rv2454c korB 2-oxoglutarate oxidoreductase subunit KorB 817 811 database:800
Rv2455c korA 2-oxoglutarate oxidoreductase subunit KorA 820 810 database:800
Rv2332 mez malate oxidoreductase 816 807 database:800
Rv1617 pykA pyruvate kinase 822 806 database:800
Rv1127c ppdK pyruvate, phosphate dikinase PpdK 806 806 database:800
Rv1872c lldD2 L-lactate dehydrogenase 803 802 database:800
Rv2241 aceE pyruvate dehydrogenase E1 component 813 801 database:800
Rv0694 mftD mycofactocin system heme/flavin oxidoreductase MftD 801 801 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-isopropylmalate dehydratase large subunit
  • MTBC0 PGAP product: 3-isopropylmalate dehydratase large subunit
  • Pfam (hmmscan --cut_ga): Aconitase PF00330.26 (E=6e-177)
  • (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_217504.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Aconitase (PF00330.26)
  • 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 COG0065
  • Curated reference: UniProt P9WQF5 (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 — 55 functional partner(s); context anchor leuD
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_003173|Rv2988c|leuC
MALQTGEPRTLAEKIWDDHIVVSGGGCAPDLIYIDLHLVHEVTSPQAFDGLRLAGRRVRRPELTLATEDHNVPTVDIDQPIADPVSRTQVETLRRNCAEFGIRLHSMGDIEQGIVHVVGPQLGLTQPGMTIVCGDSHTSTHGAFGALAMGIGTSEVEHVLATQTLPLRPFKTMAVNVDGRLPDGVSAKDIILALIAKIGTGGGQGHVIEYRGSAIESLSMEGRMTICNMSIEAGARAGMVAPDETTYAFLRGRPHAPTGAQWDTALVYWQRLRTDVGAVFDTEVYLDAASLSPFVTWGTNPGQGVPLAAAVPDPQLMTDDAERQAAEKALAYMDLRPGTAMRDIAVDAVFVGSCTNGRIEDLRVVAEVLRGRKVADGVRMLIVPGSMRVRAQAEAEGLGEIFTDAGAQWRQAGCSMCLGMNPDQLASGERCAATSNRNFEGRQGAGGRTHLVSPAVAAATAVRGTLSSPADLN