fadD4 Resolved · high auto-curated

H37Rv Rv0214 · MTBC0 - · 537 aa · 256064–257677 (+) · RefSeq NP_214728.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)fatty-acid--CoA ligase FadD4
MTBC0 PGAP re-annotation
Revised (this work)Fatty-acid--CoA ligase FadD4. 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.

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 P96396 TrEMBL · unreviewed · Evidence at protein level
UniProt nameProbable fatty-acid-CoA ligase FadD4

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Q Secondary metabolites biosynthesis, transport and catabolism
Preferred namefadD4
eggNOG descriptionActivates fatty acids by binding to coenzyme A
Orthologous groupCOG0318
EC number EC 6.2.1.3
KEGG orthology K00666, K01897
KEGG pathways map00061, map00071, map01100, map01212, map02024, map03320, map04146, map04216, map04714, map04920
KEGG modules M00086

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 0.475 · purifying
Polymorphic sites (≥ 0.1% of strains) 4 synonymous, 6 missense, 0 nonsense, 1 frameshift
Disruption 1 distinct premature-stop/frameshift site(s); most common in 0.31% of strains (444) · 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 7.7e-6642–389 AMP-binding enzyme
AMP-binding_CPF13193.13 3.8e-17447–525 AMP-binding enzyme C-terminal domain

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

Closest characterised functional partner: pckA (phosphoenolpyruvate carboxykinase), medium confidence from genomic context alone (score 654 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1550 fadD11 fatty-acid--CoA ligase FadD11 924 922 database:900
Rv2187 fadD15 long-chain-fatty-acid--CoA ligase FadD15 924 922 database:900
Rv2524c fas fatty acid synthase 924 915 database:900
Rv3097c lipY triacylglycerol lipase Lip 852 834 database:800
Rv0719 rplF 50S ribosomal protein L6 695 695 experimental:402 database:510
Rv1527c pks5 polyketide synthase 706 681
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 705 680
Rv2048c pks12 polyketide synthase 705 680
Rv2940c mas multifunctional mycocerosic acid synthase 704 679
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 704 679
Rv0211 pckA phosphoenolpyruvate carboxykinase 654 654 ctx neighborhood:544
Rv3800c pks13 polyketide synthase 668 635
Rv2946c pks1 polyketide synthase 664 632
Rv1345 mbtM long-chain-fatty-acid--ACP ligase MbtM 631 631 ctx cooccurence:631
Rv2932 ppsB phthiocerol synthesis polyketide synthase type I PpsB 629 608

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

  • Annotation from H37Rv (no MTBC0 1:1 anchor; H37Rv protein used): fatty-acid--CoA ligase FadD4
  • Pfam (hmmscan --cut_ga): AMP-binding PF00501.35 (E=8e-66), AMP-binding_C PF13193.13 (E=4e-17)
  • (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_214728.1)
  • 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 P96396 (TrEMBL, unreviewed; 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 — 85 functional partner(s); context anchor pckA
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>H37Rv|Rv0214|fadD4
MPRGELYKRFRLVMGGIAPCGSGRRAATYPRRMQIRPYIGADKPAVILYPSGTVISFDELEARANRLAHWFRQAGLREDDVVAILMENNEHVHAVMWAARRSGLYYVPINTHLTASEAAYIVDNSGAKAIVGSAALRETCHGLAEHLPGGLPDLLMLAGGGLVGWMTYPECVADQPDTPIEDEREGDLLQYSSGTTGRPKGIKRELPHVSPDAAPGMMPALLDFWMDADSVYLSPAPMYHTAPSVWTMSALAAGVTTVVMEKFDAEGALDAIQRYRVTHAQFVPAMFVRMLKLPEAVRNSYDMSSLRRVIHAAAPCPVQIKEQMIHWWGPIIDEYYASSEASGSTLITAEDWLTHPGSVGKPIQGGVHIVGADGSELPPNQPGEIYFEGGYPFEYLNDPAKTAASRNKHGWVTVGDVGYLDDDGYLFLTGRRHHMIISGGVNIYPQEAENLLVAHPKVLDAAVFGVPDDEMGQRVMAAVQTVDSADANDQFAGELLAWLRDRLSHFKCPRSIAFEPQLPRTDTGKLYKSGLVEKYSV