pks9 Resolved · high auto-curated

H37Rv Rv1664 · MTBC0 mtbc0_001772 · 1017 aa · 1900069–1903122 (+) · RefSeq NP_216180.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)polyketide synthase
MTBC0 PGAP re-annotationtype I polyketide synthase
Revised (this work)Type I polyketide synthase. Pfam: ketoacyl-synt (PF00109.33), Ketoacyl-synt_C (PF02801.29), KAsynt_C_assoc (PF16197.12), CurL-like_PKS_C (PF22621.3), Acyl_transf_1 (PF00698.27), PP-binding (PF00550.32).

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

Curated reference (UniProt)

UniProt O06586 TrEMBL · unreviewed · Evidence at protein level
UniProt nameProbable polyketide synthase Pks9

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category Q Secondary metabolites biosynthesis, transport and catabolism
Preferred namepks9
eggNOG descriptionAcyl transferase domain in polyketide synthase (PKS) enzymes.
Orthologous groupCOG3321
EC number EC 2.3.1.111, EC 2.3.1.252
KEGG orthology K11628, K12431, K12432, K12433, K12442, K12443

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 1.145 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 5 synonymous, 15 missense, 1 nonsense, 1 frameshift
Disruption 2 distinct premature-stop/frameshift site(s); most common in 0.93% of strains (1353) · 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
ketoacyl-syntPF00109.33 5.9e-5736–221 Beta-ketoacyl synthase, N-terminal domain
Ketoacyl-synt_CPF02801.29 1.3e-39230–346 Beta-ketoacyl synthase, C-terminal domain
KAsynt_C_assocPF16197.12 3.9e-13351–469 Ketoacyl-synthetase C-terminal extension
CurL-like_PKS_CPF22621.3 2.2e-07420–478 CurL-like, PKS C-terminal
Acyl_transf_1PF00698.27 1.1e-65504–778 Acyl transferase domain
PP-bindingPF00550.32 9.8e-08877–938 Phosphopantetheine attachment site

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

Closest characterised functional partner: pks17 (polyketide synthase), high confidence from genomic context alone (score 980 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1663 pks17 polyketide synthase 987 980 ctx neighborhood:781 coexpression:861
Rv1661 pks7 polyketide synthase 978 978 ctx neighborhood:855 coexpression:801
Rv1662 pks8 polyketide synthase 967 965 ctx neighborhood:781 coexpression:806
Rv1912c fadB5 oxidoreductase FadB 891 890 ctx fusion:869
Rv3777 oxidoreductase 867 866 ctx fusion:840
Rv2380c mbtE peptide synthetase 867 860 ctx fusion:562 cooccurence:558
Rv0101 nrp peptide synthetase Nrp 865 857 ctx cooccurence:580 coexpression:428
Rv2383c mbtB phenyloxazoline synthase 847 814 coexpression:408
Rv3141 fadB4 NADPH quinone oxidoreductase FadB 752 751 ctx fusion:702
Rv2379c mbtF peptide synthetase 759 750 ctx cooccurence:508
Rv2928 tesA thioesterase TesA 757 747 ctx cooccurence:696
Rv1185c fadD21 fatty-acid--CoA ligase FadD21 742 742 ctx fusion:427
Rv2930 fadD26 fatty-acid--CoA ligase FadD26 734 735 ctx fusion:418
Rv1521 fadD25 fatty-acid--CoA ligase FadD25 730 731 ctx fusion:408
Rv1529 fadD24 fatty-acid--CoA ligase FadD24 727 728

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: polyketide synthase
  • MTBC0 PGAP product: type I polyketide synthase
  • Pfam (hmmscan --cut_ga): ketoacyl-synt PF00109.33 (E=6e-57), Ketoacyl-synt_C PF02801.29 (E=1e-39), KAsynt_C_assoc PF16197.12 (E=4e-13), CurL-like_PKS_C PF22621.3 (E=2e-07), Acyl_transf_1 PF00698.27 (E=1e-65), PP-binding PF00550.32 (E=1e-07)
  • (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_216180.1)
  • Domains: Pfam-A via hmmscan --cut_ga — ketoacyl-synt (PF00109.33), Ketoacyl-synt_C (PF02801.29), KAsynt_C_assoc (PF16197.12), CurL-like_PKS_C (PF22621.3), Acyl_transf_1 (PF00698.27), PP-binding (PF00550.32)
  • 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 COG3321
  • Curated reference: UniProt O06586 (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 — 71 functional partner(s); context anchor pks17
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001772|Rv1664|pks9
MQPTGIAIIGLACRFPTVVSPGDLWDLLRDGREATGSIDNVADFDADFFNLSPREASAMDPRQRLALELTWELLEDAFVVPETLRGQPIAVYLGAMNDDYAVLTLAADRVDHHAFAGTSRAIIANRVSFAFGLRGPSVTIDSGQSSSLVAVHLACESVRTGEAPLAIAGGVHLNLARETAMLEQEFGAVSPSGHTYAFDERADGYVPGDGGGLVLLKPVQAALDDGDRIHAIIRGSAVGNAGHSATGLTVPSVAGQVDVIRRAMSGAGVDCHQVHYVEAHGTGTKIGDPIEARALGEIFAARQRRPVSVGSVKTNIGHTGGAAGIAGLLKAVLAIENAVIPPSLNYVGAPIDLDSLGLRVDTALTPWPVADEPRRAGVSSFGMGGTNAHVILEQGPTQSPEIVESVAAAGSNAPVAVPWVLAARSPQALTNQAGRLLAHLTADDGLTALDVGWSLVSTRSVFDHRAVVVGADRGRLMAGLAGLAAGEPGAGVVVGRARSVGKTVFVFPGQGSQWLGMGRQLYGRYSVFARAFDEVVAVLDGQLRLSVRQVMWGADAGLLESTEFAQPALFVVQVALAALLQDWGVLPDLVMGHSVGEIAAAYVAGALSLVDAARVVAARGRLMQALPAGGVMVAVAASEDEVAPLLTEGVCIAAVNAPESVVISGEQAAVGVVVDRLVGLGRRVRRLAVSHAFHSVLMDPMVEEFSKVLADVCVRAPRIGLVSNVTGQLAGAGYGSPAYWVEHVRKPVRFFDGVGLAESLGARVFVEVGPGAGLEASVALLARDRPEVESVLAGVGRLFAEGVAVDWSSVFAGLGGRRVELPTYGFARQRFWLGDNGELSVDQTGKDAGAIARLQSLAPPELQRQLVELVCFHAAIVLGRKSSHDIDPECAFQDLGFDSMSGVELRNRLQMAIGLPGLSLPRTLIFDYPTASALAECLGQLLGGQHESSDDESIWQLLKNIPIHQLRRTGLLDKLLLLAGQPEESLAGRTVSDEVIDSLSPEALIGLALDEDENDIR