fadE10 Family assigned · medium auto-curated

H37Rv Rv0873 · MTBC0 mtbc0_000928 · 650 aa · 973717–975669 (+) · RefSeq NP_215388.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)acyl-CoA dehydrogenase
MTBC0 PGAP re-annotationacyl-CoA dehydrogenase family protein
Revised (this work)Acyl-CoA dehydrogenase family protein. Pfam: Acyl-CoA_dh_N (PF02771.22), Acyl-CoA_dh_M (PF02770.25), Acyl-CoA_dh_1 (PF00441.30), Acyl-CoA_dh_2 (PF08028.17).

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

Curated reference (UniProt)

UniProt P9WQF7 SwissProt · reviewed · Evidence at protein level
UniProt nameProbable acyl-CoA dehydrogenase FadE10
EC (curated) EC 1.3.-.-

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Preferred namefadE10
eggNOG descriptionacyl-CoA dehydrogenase
Orthologous groupCOG1960
Gene Ontology (13) GO:0005575, GO:0005618, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0005886, GO:0016020, GO:0030312, GO:0044424, GO:0044444, GO:0044464 +1 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 0.08 · strong purifying
Polymorphic sites (≥ 0.1% of strains) 55 synonymous, 12 missense, 1 nonsense, 0 frameshift
Disruption 1 distinct premature-stop/frameshift site(s); most common in 0.78% of strains (1135) · 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_NPF02771.22 2.0e-1963–163 Acyl-CoA dehydrogenase, N-terminal domain
Acyl-CoA_dh_MPF02770.25 1.3e-20167–263 Acyl-CoA dehydrogenase, middle domain
Acyl-CoA_dh_1PF00441.30 7.4e-32277–435 Acyl-CoA dehydrogenase, C-terminal domain
Acyl-CoA_dh_2PF08028.17 5.4e-05296–398 Acyl-CoA dehydrogenase, C-terminal domain

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

PartnerProductScoreNo text-miningChannels (≥400)
Rv0860 fadB fatty oxidation protein FadB 804 788 coexpression:648
Rv3028c fixB electron transfer flavoprotein subunit alpha 713 701 coexpression:424 experimental:419
Rv3029c fixA electron transfer flavoprotein subunit beta 709 697 coexpression:412 experimental:418
Rv3153 nuoI NADH-quinone oxidoreductase subunit I 651 637
Rv0632c echA3 enoyl-CoA hydratase EchA3 606 591
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 615 585 database:459
Rv1070c echA8 enoyl-CoA hydratase EchA8 599 585
Rv2940c mas multifunctional mycocerosic acid synthase 615 584 database:459
Rv1527c pks5 polyketide synthase 614 583 database:459
Rv2048c pks12 polyketide synthase 614 583 database:459
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 613 583 database:459
Rv0905 echA6 enoyl-CoA hydratase EchA6 593 578
Rv3774 echA21 enoyl-CoA hydratase EchA21 593 578
Rv1071c echA9 enoyl-CoA hydratase EchA9 592 578
Rv0456c echA2 enoyl-CoA hydratase EchA2 592 577

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
  • MTBC0 PGAP product: acyl-CoA dehydrogenase family protein
  • Pfam (hmmscan --cut_ga): Acyl-CoA_dh_N PF02771.22 (E=2e-19), Acyl-CoA_dh_M PF02770.25 (E=1e-20), Acyl-CoA_dh_1 PF00441.30 (E=7e-32), Acyl-CoA_dh_2 PF08028.17 (E=5e-05)
  • (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_215388.1)
  • 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), Acyl-CoA_dh_2 (PF08028.17)
  • 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 P9WQF7 (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)
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_000928|Rv0873|fadE10
MAQQTQVTEEQARALAEESRESGWDKPSFAKELFLGRFPLGLIHPFPKPSDAEEARTEAFLVKLREFLDTVDGSVIERAAQIPDEYVKGLAELGCFGLKIPSEYGGLNMSQVAYNRVLMMVTTVHSSLGALLSAHQSIGVPEPLKLAGTAEQKRRFLPRCAAGAISAFLLTEPDVGSDPARMASTATPIDDGQAYELEGVKLWTTNGVVADLLVVMARVPRSEGHRGGISAFVVEADSPGITVERRNKFMGLRGIENGVTRLHRVRVPKDNLIGREGDGLKIALTTLNAGRLSLPAIATGVAKQALKIAREWSVERVQWGKPVGQHEAVASKISFIAATNYALDAVVELSSQMADEGRNDIRIEAALAKLWSSEMACLVGDELLQIRGGRGYETAESLAARGERAVPVEQMVRDLRINRIFEGSSEIMRLLIAREAVDAHLTAAGDLANPKADLRQKAAAAAGASGFYAKWLPKLVFGEGQLPTTYREFGALATHLRFVERSSRKLARNTFYGMARWQASLEKKQGFLGRIVDIGAELFAISAACVRAEAQRTADPVEGEQAYELAEAFCQQATLRVEALFDALWSNTDSIDVRLANDVLEGRYTWLEQGILDQSEGTGPWIASWEPGPSTEANLARRFLTVSPSSEAKL