fadD17 Resolved · high auto-curated

H37Rv Rv3506 · MTBC0 mtbc0_003721 · 502 aa · 3949472–3950980 (+) · RefSeq NP_218023.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)long-chain-fatty-acid--CoA ligase FadD17
MTBC0 PGAP re-annotationlong-chain-fatty-acid--CoA ligase FadD17
Revised (this work)Long-chain-fatty-acid--CoA ligase FadD17. Pfam: AMP-binding (PF00501.35), AMP-binding_C (PF13193.13).

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

Curated reference (UniProt)

UniProt O53551 SwissProt · reviewed · Evidence at protein level
UniProt nameMedium/long-chain-fatty-acid--CoA ligase FadD17
EC (curated) EC 6.2.1.2, EC 6.2.1.3
Curated functionCatalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. Also involved in steroid side-chain degradation. Activates cholesterol metabolites with a C5 side chain, including cholate and chenodeoxycholate.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Q Secondary metabolites biosynthesis, transport and catabolism
Preferred namefadD17
eggNOG descriptionActivates fatty acids by binding to coenzyme A
Orthologous groupCOG0318
KEGG orthology K00666
Gene Ontology (50) GO:0001676, GO:0003674, GO:0003824, GO:0004467, GO:0005575, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0005886, GO:0006082, GO:0006629 +38 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 0.928 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 3 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
AMP-bindingPF00501.35 1.4e-4524–353 AMP-binding enzyme
AMP-binding_CPF13193.13 1.7e-07404–480 AMP-binding enzyme C-terminal domain

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

Closest characterised functional partner: fadE26 (acyl-CoA dehydrogenase FadE26), high confidence from genomic context alone (score 823 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv3504 fadE26 acyl-CoA dehydrogenase FadE26 965 823 ctx neighborhood:768 textmining:810
Rv3505 fadE27 acyl-CoA dehydrogenase FadE27 917 808 ctx neighborhood:792 textmining:586
Rv3513c fadD18 fatty-acid--CoA ligase FadD18 853 765 ctx cooccurence:764 textmining:402
Rv3502c 3-oxoacyl-ACP reductase 784 753 ctx neighborhood:676
Rv2948c fadD22 p-hydroxybenzoyl--AMP ligase 740 740 ctx cooccurence:740
Rv0542c menE 2-succinylbenzoic acid--CoA ligase 728 728 ctx cooccurence:727
Rv0719 rplF 50S ribosomal protein L6 695 695 experimental:402 database:510
Rv1527c pks5 polyketide synthase 706 681
Rv2048c pks12 polyketide synthase 705 680
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 705 680
Rv2940c mas multifunctional mycocerosic acid synthase 743 679
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 704 679
Rv3800c pks13 polyketide synthase 690 635
Rv2946c pks1 polyketide synthase 664 632
Rv1181 pks4 polyketide beta-ketoacyl synthase 654 608

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: long-chain-fatty-acid--CoA ligase FadD17
  • MTBC0 PGAP product: long-chain-fatty-acid--CoA ligase FadD17
  • Pfam (hmmscan --cut_ga): AMP-binding PF00501.35 (E=1e-45), AMP-binding_C PF13193.13 (E=2e-07)
  • (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_218023.1)
  • Domains: Pfam-A via hmmscan --cut_ga — AMP-binding (PF00501.35), AMP-binding_C (PF13193.13)
  • 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 O53551 (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 — 106 functional partner(s); context anchor fadE26
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_003721|Rv3506|fadD17
MTPTHPTVTELLLPLSEIDDRGVYFEDSFTSWRDHIRHGAAIAAALRERLDPARPPHVGVLLQNTPFFSATLVAGALSGIVPVGLNPVRRGAALAGDIAKADCQLVLTGSGSAEVPADVEHINVDSPEWTDEVAAHRDTEVRFRSADLADLFMLIFTSGTSGDPKAVKCSHRKVAIAGVTITQRFSLGRDDVCYVSMPLFHSNAVLVGWAVAAACQGSMALRRKFSASQFLADVRRYGATYANYVGKPLSYVLATPELPDDADNPLRAVYGNEGVPGDIDRFGRRFGCVVMDGFGSTEGGVAITRTLDTPAGALGPLPGGIQIVDPDTGEPCPTGVVGELVNTAGPGGFEGYYNDEAAEAERMAGGVYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLMRYPDATEVAVYPVPDPVVGDQVMAALVLAPGTKFDADKFRAFLTEQPDLGHKQWPSYVRVSAGLPRTMTFKVIKRQLSAEGVACADPVWPIRR