fadE8 Family assigned · medium auto-curated

H37Rv Rv0672 · MTBC0 mtbc0_000711 · 542 aa · 775570–777198 (+) · RefSeq NP_215186.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)acyl-CoA dehydrogenase FadE8
MTBC0 PGAP re-annotationacyl-CoA dehydrogenase family protein
Revised (this work)Acyl-CoA dehydrogenase family protein. Pfam: AidB_N (PF18158.7), 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 I6X9J0 TrEMBL · unreviewed · Evidence at protein level
UniProt nameProbable acyl-CoA dehydrogenase FadE8

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Preferred nameaidB
eggNOG descriptionacyl-CoA dehydrogenase
Orthologous groupCOG1960
KEGG orthology K09456

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) pseudogene candidate

pN/pS 0.194 · strong purifying
Polymorphic sites (≥ 0.1% of strains) 7 synonymous, 4 missense, 0 nonsense, 1 frameshift
Disruption 1 distinct premature-stop/frameshift site(s); most common in 1.40% of strains (2032) · 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
AidB_NPF18158.7 3.4e-539–162 Adaptive response protein AidB N-terminal domain
Acyl-CoA_dh_MPF02770.25 4.0e-16177–269 Acyl-CoA dehydrogenase, middle domain
Acyl-CoA_dh_1PF00441.30 4.1e-28280–434 Acyl-CoA dehydrogenase, C-terminal domain
Acyl-CoA_dh_2PF08028.17 6.6e-08298–419 Acyl-CoA dehydrogenase, C-terminal domain

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

Closest characterised functional partner: echA4 (enoyl-CoA hydratase EchA4), high confidence from genomic context alone (score 992 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0673 echA4 enoyl-CoA hydratase EchA4 997 992 ctx neighborhood:874 coexpression:900 textmining:657
Rv0675 echA5 enoyl-CoA hydratase EchA5 959 958 ctx neighborhood:874 coexpression:487
Rv0674 hyp hypothetical protein 875 876 ctx neighborhood:874
Rv0860 fadB fatty oxidation protein FadB 864 853 coexpression:647
Rv0670 end endonuclease IV 769 769 ctx neighborhood:768
Rv3028c fixB electron transfer flavoprotein subunit alpha 667 653 coexpression:410 experimental:419
Rv3029c fixA electron transfer flavoprotein subunit beta 664 650 coexpression:406 experimental:418
Rv0241c htdX 3-hydroxyacyl-thioester dehydratase HtdX 648 648
Rv0671 lpqP lipoprotein LpqP 646 646 ctx neighborhood:641
Rv3153 nuoI NADH-quinone oxidoreductase subunit I 652 638
Rv0632c echA3 enoyl-CoA hydratase EchA3 648 635
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 617 587 database:459
Rv2048c pks12 polyketide synthase 617 587 database:459
Rv2940c mas multifunctional mycocerosic acid synthase 615 585 database:459
Rv1527c pks5 polyketide synthase 615 584 database:459

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 FadE8
  • MTBC0 PGAP product: acyl-CoA dehydrogenase family protein
  • Pfam (hmmscan --cut_ga): AidB_N PF18158.7 (E=3e-53), Acyl-CoA_dh_M PF02770.25 (E=4e-16), Acyl-CoA_dh_1 PF00441.30 (E=4e-28), Acyl-CoA_dh_2 PF08028.17 (E=7e-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_215186.1)
  • Domains: Pfam-A via hmmscan --cut_ga — AidB_N (PF18158.7), 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 I6X9J0 (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 — 120 functional partner(s); context anchor echA4
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_000711|Rv0672|fadE8
MSDTHVVTNQVPPLENYNPASSPVLIEALIQEGGQWGLDEVNEVGAISASCQAQRWGELADRNRPILHTHDAYGYRVDEVEYDPAYHELMRTAITHGMHAAPWADDRPGAHVVRAAKTSVWTVEPGHICPISMTYAVVPALRYNSELAAVYEPLLTSREYDPELKPATTKAGITAGMSMTEKQGGSDVRAGTTQATPNADGSYSLTGHKWFTSAPMCDIFLVLAQAPDGLSCFLLPRVLPDGTRNRMFLQRLKDKLGNHANASSEVEYDGAVAWLVGEEGRGVPTIIEMVNLTRLDCALGSATSMRTGLTRAVHHAQHRKAFGAYLIDQPLMRNVLADLAVEAEAATIVAMRMAGATDNAVRGNETEALLRRIGLAAAKYWVCKRSTAHAAEALECLGGNGYVEDSGMPRLYREAPLMGIWEGSGNVSALDTLRAMATRPACVEVLFDELARSAGQDPRLDGHVERLRPQLGDLDTIGYRARKIAEDICLALQGSLLVRHGHPAVAEAFLATRLGGQWGGAYGTMPAGLDLAPILERALVKG