fadE17 Resolved · high auto-curated

H37Rv Rv1934c · MTBC0 mtbc0_002048 · 409 aa · 2204075–2205304 (-) · RefSeq NP_216450.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)acyl-CoA dehydrogenase FadE17
MTBC0 PGAP re-annotationacyl-CoA dehydrogenase
Revised (this work)Acyl-CoA dehydrogenase. Pfam: Acyl-CoA_dh_N (PF02771.22), Acyl-CoA_dh_M (PF02770.25), Acyl-CoA_dh_1 (PF00441.30).

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

Curated reference (UniProt)

UniProt P95280 SwissProt · reviewed · Evidence at transcript level
UniProt namePutative acyl-CoA dehydrogenase FadE17
EC (curated) EC 1.3.99.-

UniProt still lists this protein as Putative acyl-CoA dehydrogenase FadE17; the revised annotation above is ahead of the current UniProt record.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category C Energy production and conversion
Preferred namefadE17
eggNOG descriptionacyl-CoA dehydrogenase
Orthologous groupCOG1960
Gene Ontology (6) GO:0005575, GO:0005618, GO:0005623, GO:0030312, GO:0044464, GO:0071944

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 0.799 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 5 synonymous, 11 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
Acyl-CoA_dh_NPF02771.22 6.1e-227–124 Acyl-CoA dehydrogenase, N-terminal domain
Acyl-CoA_dh_MPF02770.25 1.0e-20128–220 Acyl-CoA dehydrogenase, middle domain
Acyl-CoA_dh_1PF00441.30 2.7e-20234–397 Acyl-CoA dehydrogenase, C-terminal domain

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

Closest characterised functional partner: echA13 (enoyl-CoA hydratase EchA13), high confidence from genomic context alone (score 991 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1935c echA13 enoyl-CoA hydratase EchA13 993 991 ctx neighborhood:869 coexpression:900
Rv1933c fadE18 acyl-CoA dehydrogenase FadE18 984 963 ctx neighborhood:782 cooccurence:773 textmining:586
Rv3564 fadE33 acyl-CoA dehydrogenase FadE33 925 834 ctx cooccurence:773 textmining:571
Rv1966 mce3A Mce family protein Mce3A 804 804 coexpression:804
Rv1965 yrbE3B integral membrane protein 788 788 coexpression:788
Rv0860 fadB fatty oxidation protein FadB 802 786 coexpression:645
Rv3563 fadE32 acyl-CoA dehydrogenase FadE32 834 784 ctx cooccurence:755
Rv1968 mce3C Mce family protein Mce3C 780 780 coexpression:780
Rv3029c fixA electron transfer flavoprotein subunit beta 769 759 coexpression:406 experimental:418
Rv1969 mce3D Mce family protein Mce3D 754 754 coexpression:754
Rv3028c fixB electron transfer flavoprotein subunit alpha 763 753 coexpression:412 experimental:419
Rv1937 oxygenase 763 749 ctx neighborhood:528
Rv3505 fadE27 acyl-CoA dehydrogenase FadE27 808 739 ctx cooccurence:738
Rv1967 mce3B Mce family protein Mce3B 734 734 coexpression:734
Rv1679 fadE16 acyl-CoA dehydrogenase FadE16 706 706 ctx cooccurence:702

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 FadE17
  • MTBC0 PGAP product: acyl-CoA dehydrogenase
  • Pfam (hmmscan --cut_ga): Acyl-CoA_dh_N PF02771.22 (E=6e-22), Acyl-CoA_dh_M PF02770.25 (E=1e-20), Acyl-CoA_dh_1 PF00441.30 (E=3e-20)
  • (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_216450.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Acyl-CoA_dh_N (PF02771.22), Acyl-CoA_dh_M (PF02770.25), Acyl-CoA_dh_1 (PF00441.30)
  • 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 P95280 (SwissProt, reviewed; Evidence at transcript 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 — 129 functional partner(s); context anchor echA13
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_002048|Rv1934c|fadE17
MDVSYPPEAEAFRDRIREFVAEHLPPGWPGPGALPPHEREEFARHWRRALAGAGLVAVSWPTEYGGGGLSPMEQVVLAEEFARAGAPERAENDLLGIDLLGNTLIALGSEAQKRHFLPRILSGEHRWCQGFSEPEAGSDLASVRTRGVLDGDEWVINGHKIWTSAGTTANWIFLLARTDPSAAKHRGLSFLLVPMDQPGVVVRPIVNAAGHSSFSEVFLTDARTSAGNVVGRVGDGWSTAMTLLGFERGSHIATAAIDFERDLQRLCELARDRGLHTDPRVRDGLAWCYARVQIMRYRGYRDLTLALTGRPPGAEAAITKVIWSEYFRRYTDLAVEILGLEALGPRGPGNGGARLVPEAGTPNSPACWMDELLYARAATIYAGSSQIQRNVIGERLLGLPKEPRPEVLC