fadE5 Resolved · high auto-curated

H37Rv Rv0244c · MTBC0 mtbc0_000260 · 611 aa · 294180–296015 (-) · RefSeq NP_214758.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)acyl-CoA dehydrogenase FadE5
MTBC0 PGAP re-annotationacyl-CoA dehydrogenase
Revised (this work)Acyl-CoA dehydrogenase. Pfam: Acyl-CoA_dh_M (PF02770.25), Acyl-CoA_dh_1 (PF00441.30), Acyl-CoA_dh_C (PF12806.13).

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

Curated reference (UniProt)

UniProt O53666 SwissProt · reviewed · Evidence at protein level
UniProt nameBroad-specificity linear acyl-CoA dehydrogenase FadE5
EC (curated) EC 1.3.8.1, EC 1.3.8.7, EC 1.3.8.8
Curated functionAcyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Preferred namefadE5
eggNOG descriptionacyl-CoA dehydrogenase
Orthologous groupCOG1960

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 0.448 · purifying
Polymorphic sites (≥ 0.1% of strains) 10 synonymous, 14 missense, 0 nonsense, 1 frameshift
Disruption 1 distinct premature-stop/frameshift site(s); most common in 0.73% of strains (1060) · 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
Acyl-CoA_dh_MPF02770.25 4.1e-14162–271 Acyl-CoA dehydrogenase, middle domain
Acyl-CoA_dh_1PF00441.30 1.0e-12288–454 Acyl-CoA dehydrogenase, C-terminal domain
Acyl-CoA_dh_CPF12806.13 5.2e-30475–607 Acetyl-CoA dehydrogenase C-terminal like

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

Closest characterised functional partner: Rv3679 (anion transporter ATPase), medium confidence from genomic context alone (score 685 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0860 fadB fatty oxidation protein FadB 909 793 coexpression:656 textmining:581
Rv3028c fixB electron transfer flavoprotein subunit alpha 783 774 coexpression:410 experimental:419
Rv0487 hyp hypothetical protein 746 747 ctx cooccurence:745
Rv3029c fixA electron transfer flavoprotein subunit beta 743 732 coexpression:408 experimental:418
Rv3679 anion transporter ATPase 684 685 ctx cooccurence:682
Rv3680 anion transporter ATPase 638 638 ctx cooccurence:635
Rv3153 nuoI NADH-quinone oxidoreductase subunit I 649 634
Rv0632c echA3 enoyl-CoA hydratase EchA3 646 633
Rv0971c echA7 enoyl-CoA hydratase EchA7 640 627
Rv2940c mas multifunctional mycocerosic acid synthase 634 588 database:459
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 619 588 database:459
Rv2048c pks12 polyketide synthase 617 587 database:459
Rv1527c pks5 polyketide synthase 615 585 database:459
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 714 584 database:459
Rv0905 echA6 enoyl-CoA hydratase EchA6 646 578

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: acyl-CoA dehydrogenase FadE5
  • MTBC0 PGAP product: acyl-CoA dehydrogenase
  • Pfam (hmmscan --cut_ga): Acyl-CoA_dh_M PF02770.25 (E=4e-14), Acyl-CoA_dh_1 PF00441.30 (E=1e-12), Acyl-CoA_dh_C PF12806.13 (E=5e-30)
  • (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_214758.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Acyl-CoA_dh_M (PF02770.25), Acyl-CoA_dh_1 (PF00441.30), Acyl-CoA_dh_C (PF12806.13)
  • 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 COG1960
  • Curated reference: UniProt O53666 (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 — 126 functional partner(s); context anchor Rv3679
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_000260|Rv0244c|fadE5
MSHYRSNVRDQVFNLFEVLGVDKALGHGEFSDVDVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFDPKTHSVMLPESFKKSVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAGGAGFAQILYHLGTEEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDVETGEPGERNGVFVTNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGADLTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDAAVAEVVHGVDAKLAVKVNDLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDFFFRKIVRDKGVALAHVSGQIQEFVDSGAGNGRLKTERALLAKALTDVQGMAAALTGYLMAAQQDVTSLYKVGLGSVRFLMSVGDLIIGWLLQRQAAVAVAALDAGATGDERSFYEGKVAVASFFAKNFLPLLTSTREVIETLDNDIMELDEAAF