fadD30 Resolved · high auto-curated

H37Rv Rv0404 · MTBC0 - · 585 aa · 483977–485734 (+) · RefSeq NP_214918.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)long-chain-fatty-acid--AMP ligase FadD30
MTBC0 PGAP re-annotation
Revised (this work)Long-chain-fatty-acid--AMP ligase FadD30. Pfam: AMP-binding (PF00501.35), AMP-dom_DIP2-like (PF23024.2).

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

Annotated on the H37Rv protein: this gene has no 1:1 ancestral MTBC0 anchor (PE/PPE, paralogue, IS element, or otherwise unanchored CDS).

Curated reference (UniProt)

UniProt P9WQ57 SwissProt · reviewed · Evidence at protein level
UniProt nameProbable long-chain-fatty-acid--AMP ligase FadD30
EC (curated) EC 6.2.1.-
Curated functionCatalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to a multifunctional polyketide synthase (PKS) for further chain extension.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category F Nucleotide transport and metabolism
Preferred namefadD30
eggNOG descriptionCatalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase (PKS) for further chain extension
Orthologous groupCOG0318
Gene Ontology (75) GO:0002682, GO:0002684, GO:0003674, GO:0003824, GO:0005575, GO:0005623, GO:0005886, GO:0006082, GO:0006629, GO:0006631, GO:0006633, GO:0008150 +63 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 0.689 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 8 synonymous, 16 missense, 1 nonsense, 1 frameshift
Disruption 2 distinct premature-stop/frameshift site(s); most common in 0.23% of strains (330) · clonal

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
AMP-bindingPF00501.35 4.0e-508–418 AMP-binding enzyme
AMP-dom_DIP2-likePF23024.2 2.6e-08467–580 Disco-interacting protein 2-like, AMP domain

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

Closest characterised functional partner: pks6 (membrane bound polyketide synthase), high confidence from genomic context alone (score 988 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0405 pks6 membrane bound polyketide synthase 988 988 ctx neighborhood:810 coexpression:810
Rv2380c mbtE peptide synthetase 937 934 ctx fusion:586 cooccurence:651 experimental:465
Rv2379c mbtF peptide synthetase 821 819 ctx cooccurence:604
Rv0101 nrp peptide synthetase Nrp 781 770 ctx cooccurence:634
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 762 742
Rv1527c pks5 polyketide synthase 757 737
Rv2932 ppsB phthiocerol synthesis polyketide synthase type I PpsB 751 737
Rv2940c mas multifunctional mycocerosic acid synthase 754 733
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 752 731
Rv2931 ppsA phthiocerol synthesis polyketide synthase type I PpsA 731 721
Rv1180 pks3 polyketide beta-ketoacyl synthase 714 714
Rv3800c pks13 polyketide synthase 738 712
Rv2947c pks15 polyketide synthase 710 710
Rv0719 rplF 50S ribosomal protein L6 699 699 experimental:402 database:510
Rv2382c mbtC polyketide synthetase 686 686

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

  • Annotation from H37Rv (no MTBC0 1:1 anchor; H37Rv protein used): long-chain-fatty-acid--AMP ligase FadD30
  • Pfam (hmmscan --cut_ga): AMP-binding PF00501.35 (E=4e-50), AMP-dom_DIP2-like PF23024.2 (E=3e-08)
  • (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_214918.1)
  • Domains: Pfam-A via hmmscan --cut_ga — AMP-binding (PF00501.35), AMP-dom_DIP2-like (PF23024.2)
  • 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 COG0318
  • Curated reference: UniProt P9WQ57 (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 — 88 functional partner(s); context anchor pks6
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>H37Rv|Rv0404|fadD30
MSVISTLRDRATTTPSDEAFVFMDYDTKTGDQIDRMTWSQLYSRVTAVSAYLISYGRHADRRRTAAISAPQGLDYVAGFLGALCAGWTPVPLPEPLGSLRDKRTGLAVLDCAADVVLTTSQAETRVRATIATHGASVTTPVIALDTLDEPSGDNCDLDSQLSDWSSYLQYTSGSTANPRGVVLSMRNVTENVDQIIRNYFRHEGGAPRLPSSVVSWLPLYHDMGLMVGLFIPLFVGCPVILTSPEAFIRKPARWMQLLAKHQAPFSAAPNFAFDLAVAKTSEEDMAGLDLGHVNTIINGAEQVQPNTITKFLRRFRPYNLMPAAVKPSYGMAEAVVYLATTKAGSPPTSTEFDADSLARGHAELSTFETERATRLIRYHSDDKEPLLRIVDPDSNIELGPGRIGEIWIHGKNVSTGYHNADDALNRDKFQASIREASAGTPRSPWLRTGDLGFIVGDEFYIVGRMKDLIIQDGVNHYPDDIETTVKEFTGGRVAAFSVSDDGVEHLVIAAEVRTEHGPDKVTIMDFSTIKRLVVSALSKLHGLHVTDFLLVPPGALPKTTSGKISRAACAKQYGANKLQRVATFP