fadD25 Resolved · high auto-curated

H37Rv Rv1521 · MTBC0 mtbc0_001628 · 583 aa · 1722111–1723862 (+) · RefSeq NP_216037.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)fatty-acid--CoA ligase FadD25
MTBC0 PGAP re-annotationfatty-acid--AMP ligase FAAL25/FadD25
Revised (this work)Fatty-acid--AMP ligase FAAL25/FadD25. 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.

Curated reference (UniProt)

UniProt P9WQ45 SwissProt · reviewed · Evidence at protein level
UniProt namePutative fatty-acid--CoA ligase fadD25
EC (curated) EC 6.2.1.-

UniProt still lists this protein as Putative fatty-acid--CoA ligase fadD25; the revised annotation above is ahead of the current UniProt record.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Q Secondary metabolites biosynthesis, transport and catabolism
Preferred namefadD25
eggNOG descriptionActivates fatty acids by binding to coenzyme A
Orthologous groupCOG0318
EC number EC 2.7.7.95, EC 6.2.1.51
KEGG orthology K00666, K12423, K12425, K12426, K12427, K12428, K21059
Gene Ontology (35) GO:0003674, GO:0003824, GO:0005575, GO:0005623, GO:0005886, GO:0006082, GO:0006629, GO:0006631, GO:0006633, GO:0008150, GO:0008152, GO:0008610 +23 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 0.444 · purifying
Polymorphic sites (≥ 0.1% of strains) 6 synonymous, 8 missense, 0 nonsense, 2 frameshift
Disruption 2 distinct premature-stop/frameshift site(s); most common in 0.24% of strains (351) · 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 7.2e-5613–419 AMP-binding enzyme
AMP-dom_DIP2-likePF23024.2 3.4e-08467–578 Disco-interacting protein 2-like, AMP domain

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

Closest characterised functional partner: mbtE (peptide synthetase), high confidence from genomic context alone (score 955 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv2380c mbtE peptide synthetase 957 955 ctx fusion:692 cooccurence:682 experimental:465
Rv2379c mbtF peptide synthetase 869 868 ctx fusion:506 cooccurence:642
Rv2947c pks15 polyketide synthase 813 813 ctx fusion:585
Rv0101 nrp peptide synthetase Nrp 806 797 ctx cooccurence:662
Rv2383c mbtB phenyloxazoline synthase 789 767 ctx fusion:510
Rv1180 pks3 polyketide beta-ketoacyl synthase 761 762 ctx fusion:454
Rv0405 pks6 membrane bound polyketide synthase 771 760
Rv2932 ppsB phthiocerol synthesis polyketide synthase type I PpsB 772 759
Rv2382c mbtC polyketide synthetase 761 753 ctx fusion:474
Rv1527c pks5 polyketide synthase 769 747
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 768 746
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 765 745
Rv2940c mas multifunctional mycocerosic acid synthase 765 741
Rv1664 pks9 polyketide synthase 730 731 ctx fusion:408
Rv2931 ppsA phthiocerol synthesis polyketide synthase type I PpsA 736 726

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: fatty-acid--CoA ligase FadD25
  • MTBC0 PGAP product: fatty-acid--AMP ligase FAAL25/FadD25
  • Pfam (hmmscan --cut_ga): AMP-binding PF00501.35 (E=7e-56), 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_216037.1)
  • 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 P9WQ45 (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 — 84 functional partner(s); context anchor mbtE
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001628|Rv1521|fadD25
MSVVESSLPGVLRERASFQPNDKALTFIDYERSWDGVEETLTWSQLYRRTLNLAAQLREHGSTGDRALILAPQSLDYVVSFIASLQAGIVAVPLSIPQGGAHDERTVSVFADTAPAIVLTASSVVDNVVEYVQPQPGQNAPAVIEVDRLDLDARPSSGSRSAAHGHPDILYLQYTSGSTRTPAGVMVSNKNLFANFEQIMTSYYGVYGKVAPPGSTVVSWLPFYHDMGFVLGLILPILAGIPAVLTSPIGFLQRPARWIQMLASNTLAFTAAPNFAFDLASRKTKDEDMEGLDLGGVHGILNGSERVQPVTLKRFIDRFAPFNLDPKAIRPSYGMAEATVYVATRKAGQPPKIVQFDPQKLPDGQAERTESDGGTPLVSYGIVDTQLVRIVDPDTGIERPAGTIGEIWVHGDNVAIGYWQKPEATERTFSATIVNPSEGTPAGPWLRTGDSGFLSEGELFIMGRIKDLLIVYGRNHSPDDIEATIQTISPGRCAAIAVSEHGAEKLVAIIELKKKDESDDEAAERLGFVKREVTSAISKSHGLSVADLVLVSPGSIPITTSGKIRRAQCVELYRQDEFTRLDA