lipB Resolved · high auto-curated

H37Rv Rv2217 · MTBC0 mtbc0_002353 · 230 aa · 2510741–2511433 (+) · RefSeq NP_216733.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)octanoyltransferase
MTBC0 PGAP re-annotationlipoyl(octanoyl) transferase LipB
Revised (this work)Lipoyl(octanoyl) transferase LipB. Pfam: LplA-B_cat (PF21948.2).

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

Curated reference (UniProt)

UniProt P9WK83 SwissProt · reviewed · Evidence at protein level
UniProt nameOctanoyltransferase
EC (curated) EC 2.3.1.181
Curated functionCatalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category H Coenzyme transport and metabolism
Preferred namelipB
eggNOG descriptionCatalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate
Orthologous groupCOG0321
EC number EC 2.3.1.181
KEGG orthology K03801
KEGG pathways map00785, map01100
Gene Ontology (63) GO:0003674, GO:0003824, GO:0005575, GO:0005623, GO:0005886, GO:0006082, GO:0006464, GO:0006629, GO:0006631, GO:0006633, GO:0006732, GO:0006790 +51 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 0.787 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 2 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
LplA-B_catPF21948.2 1.4e-4521–206 Lipoyl protein ligase A/B catalytic domain

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

Closest characterised functional partner: lipA (lipoyl synthase), high confidence from genomic context alone (score 1000 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv2218 lipA lipoyl synthase 999 1000 ctx neighborhood:882 fusion:900 cooccurence:762 database:900 textmining:892
Rv2215 dlaT pyruvate dehydrogenase E2 component dihydrolipoamide acyltransferase 943 916 ctx neighborhood:808 cooccurence:505
Rv1826 gcvH glycine cleavage system protein H 954 891 database:844 textmining:596
Rv2219 transmembrane protein 846 847 ctx neighborhood:843
Rv2524c fas fatty acid synthase 847 827 database:800
Rv2216 epimerase family protein 871 817 ctx neighborhood:808
Rv2946c pks1 polyketide synthase 710 667 database:574
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 707 663 database:574
Rv2940c mas multifunctional mycocerosic acid synthase 707 663 database:574
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 706 663 database:574
Rv1527c pks5 polyketide synthase 706 662 database:574
Rv2048c pks12 polyketide synthase 706 662 database:574
Rv1181 pks4 polyketide beta-ketoacyl synthase 686 650 database:574
Rv1661 pks7 polyketide synthase 685 649 database:574
Rv2932 ppsB phthiocerol synthesis polyketide synthase type I PpsB 678 645 database:574

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: octanoyltransferase
  • MTBC0 PGAP product: lipoyl(octanoyl) transferase LipB
  • Pfam (hmmscan --cut_ga): LplA-B_cat PF21948.2 (E=1e-45)
  • (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_216733.1)
  • Domains: Pfam-A via hmmscan --cut_ga — LplA-B_cat (PF21948.2)
  • 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 COG0321
  • Curated reference: UniProt P9WK83 (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 — 46 functional partner(s); context anchor lipA
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_002353|Rv2217|lipB
MTGSIRSKLSAIDVRQLGTVDYRTAWQLQRELADARVAGGADTLLLLEHPAVYTAGRRTETHERPIDGTPVVDTDRGGKITWHGPGQLVGYPIIGLAEPLDVVNYVRRLEESLIQVCADLGLHAGRVDGRSGVWLPGRPARKVAAIGVRVSRATTLHGFALNCDCDLAAFTAIVPCGISDAAVTSLSAELGRTVTVDEVRATVAAAVCAALDGVLPVGDRVPSHAVPSPL