fadD11 Resolved · high auto-curated

H37Rv Rv1550 · MTBC0 - · 571 aa · 1753716–1755431 (+) · RefSeq NP_216066.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)fatty-acid--CoA ligase FadD11
MTBC0 PGAP re-annotation
Revised (this work)Fatty-acid--CoA ligase FadD11. Pfam: AMP-binding (PF00501.35), AMP-binding_C_3 (PF23562.3).

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 P9WQ53 SwissProt · reviewed · Inferred from homology
UniProt namePutative fatty-acid--CoA ligase fadD11
EC (curated) EC 6.2.1.-

UniProt still lists this protein as Putative fatty-acid--CoA ligase fadD11; the revised annotation above is ahead of the current UniProt record.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Preferred namefadD11
eggNOG descriptionsynthetase
Orthologous groupCOG1022
Gene Ontology (8) GO:0005575, GO:0005618, GO:0005623, GO:0005886, GO:0016020, 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) pseudogene candidate

pN/pS 0.405 · purifying
Polymorphic sites (≥ 0.1% of strains) 7 synonymous, 8 missense, 0 nonsense, 1 frameshift
Disruption 1 distinct premature-stop/frameshift site(s); most common in 29.48% of strains (42805) · 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 1.2e-41126–379 AMP-binding enzyme
AMP-binding_C_3PF23562.3 1.3e-09419–553 AMP-binding enzyme C-terminal domain

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

Closest characterised functional partner: fadD11.1 (Possible fatty-acid-CoA ligase FadD11.1 (fatty-acid-CoA synthetase) (fatty-acid-CoA synthase); Rv1549, (MTCY48.16c), len: 175 aa. Possible f), high confidence from genomic context alone (score 999 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1549 fadD11.1 Possible fatty-acid-CoA ligase FadD11.1 (fatty-acid-CoA synthetase) (fatty-acid-CoA synthase); Rv1549, (MTCY48.16c), len: 175 aa. Possible f 999 999 ctx neighborhood:781 fusion:900 cooccurence:745 coexpression:838
Rv1551 plsB1 acyltransferase PlsB 972 971 ctx neighborhood:812 coexpression:853
Rv2524c fas fatty acid synthase 951 932 database:900
Rv2187 fadD15 long-chain-fatty-acid--CoA ligase FadD15 923 923 database:900
Rv0214 fadD4 fatty-acid--CoA ligase FadD4 924 922 database:900
Rv3097c lipY triacylglycerol lipase Lip 809 803 database:800
Rv2485c lipQ carboxylesterase LipQ 807 800 coexpression:799
Rv0458 aldehyde dehydrogenase 702 691 coexpression:663
Rv1389 gmk guanylate kinase 642 643 database:591
Rv0270 fadD2 fatty-acid--CoA ligase FadD2 654 642 ctx cooccurence:627
Rv0009 ppiA iron-regulated peptidyl-prolyl cis-trans isomerase PpiA 569 568 database:428
Rv0166 fadD5 fatty-acid--CoA ligase FadD5 561 546 coexpression:410
Rv1548c PPE21 PPE family protein PPE21 528 528 ctx neighborhood:524
Rv0526 thioredoxin 509 500
Rv2582 ppiB peptidyl-prolyl cis-trans isomerase B 495 496 database:428

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 FadD11
  • Pfam (hmmscan --cut_ga): AMP-binding PF00501.35 (E=1e-41), AMP-binding_C_3 PF23562.3 (E=1e-09)
  • (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_216066.1)
  • Domains: Pfam-A via hmmscan --cut_ga — AMP-binding (PF00501.35), AMP-binding_C_3 (PF23562.3)
  • 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 COG1022
  • Curated reference: UniProt P9WQ53 (SwissProt, reviewed; Inferred from homology)
  • 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 — 63 functional partner(s); context anchor fadD11.1
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>H37Rv|Rv1550|fadD11
MARLRGAGAAGRCRPGRFGSSARRHGLADDGEPDRVLPARRRCSARRRHLVFGVQHPARRAADLRVRQRGDQGGHLRATVRRSRSRQRCAHRTHRLRRWRAPGTLSLTDLYAAASGDFFDFESTWRAVQPEDIVTLIYTSGTTGNPKGVEMTHANLLFEGYAIDEVLGIRFGDRVTSFLPSAHIADRMTGLYLQEMFGTQVTAVADARTIAAALPDVRPTVWGAVPRVWEKLKAGIEFTVARETDEMKRQALAWAMSVAGKRANALLAGESMSDQLVAEWAKADELVLSKLRERLGFGELRWALSGAAPIPKETLAFFAGIGIPIAEIWGMSELSCVATASHPRDGRLGTVGKLLPGLQGKIAEDGEYLVRGPLVMKGYRKEPAKTAEAIDSDGWLHTGDVFDIDSDGYLRVVDRKKELIINAAGKNMSPANIENTILAACPMVGVMMAIGDGRTYNTALLVFDADSLGPYAAQRGLDASPAALAADPEVIARIAAGVAEGNAKLSRVEQIKRFRILPTLWEPGGDEITLTMKLKRRRIAAKYSAEIEELYASELRPQVYEPAAVPSTQPA