fadD22 Resolved · high auto-curated

H37Rv Rv2948c · MTBC0 mtbc0_003130 · 705 aa · 3319012–3321129 (-) · RefSeq NP_217464.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)p-hydroxybenzoyl--AMP ligase
MTBC0 PGAP re-annotationp-hydroxybenzoic acid--AMP ligase FadD22
Revised (this work)P-hydroxybenzoic acid--AMP ligase FadD22. Pfam: AMP-binding (PF00501.35), AMP-binding_C (PF13193.13), 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 P9WQ61 SwissProt · reviewed · Evidence at protein level
UniProt namep-hydroxybenzoic acid--AMP ligase FadD22
EC (curated) EC 6.2.1.50
Curated functionCatalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. Usually, this intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1, but M.tuberculosis lacks Pks15/1 due to a natural frameshift and thus is unable to produce PPOL.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Q Secondary metabolites biosynthesis, transport and catabolism
Preferred namefadD22
eggNOG descriptionCatalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22
Orthologous groupCOG0236
EC number EC 6.2.1.50
KEGG orthology K12424
Gene Ontology (47) GO:0003674, GO:0003824, GO:0006066, GO:0006629, GO:0006643, GO:0006664, GO:0006725, GO:0008150, GO:0008152, GO:0008610, GO:0009058, GO:0009247 +35 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 0.291 · purifying
Polymorphic sites (≥ 0.1% of strains) 11 synonymous, 8 missense, 1 nonsense, 1 frameshift
Disruption 2 distinct premature-stop/frameshift site(s); most common in 0.36% of strains (526) · 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 1.3e-6217–354 AMP-binding enzyme
AMP-binding_CPF13193.13 4.1e-11402–480 AMP-binding enzyme C-terminal domain
PP-bindingPF00550.32 8.2e-07549–615 Phosphopantetheine attachment site

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

Closest characterised functional partner: Rv2949c (chorismate pyruvate-lyase), high confidence from genomic context alone (score 981 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv2949c chorismate pyruvate-lyase 987 981 ctx neighborhood:739 coexpression:839 database:500
Rv2947c pks15 polyketide synthase 980 973 ctx neighborhood:774 coexpression:817
Rv2950c fadD29 long-chain-fatty-acid--AMP ligase FadD29 954 939 ctx neighborhood:666 coexpression:791
Rv2946c pks1 polyketide synthase 951 934 ctx neighborhood:799
Rv2940c mas multifunctional mycocerosic acid synthase 927 911 coexpression:778
Rv2932 ppsB phthiocerol synthesis polyketide synthase type I PpsB 903 891 coexpression:770
Rv3513c fadD18 fatty-acid--CoA ligase FadD18 769 769 ctx cooccurence:769
Rv3506 fadD17 long-chain-fatty-acid--CoA ligase FadD17 740 740 ctx cooccurence:740
Rv2939 papA5 phthiocerol/phthiodiolone dimycocerosyl transferase 760 730 coexpression:730
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 816 719
Rv0719 rplF 50S ribosomal protein L6 781 708 experimental:402 database:510
Rv2048c pks12 polyketide synthase 746 698
Rv2931 ppsA phthiocerol synthesis polyketide synthase type I PpsA 752 688
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 737 681
Rv1527c pks5 polyketide synthase 706 681

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: p-hydroxybenzoyl--AMP ligase
  • MTBC0 PGAP product: p-hydroxybenzoic acid--AMP ligase FadD22
  • Pfam (hmmscan --cut_ga): AMP-binding PF00501.35 (E=1e-62), AMP-binding_C PF13193.13 (E=4e-11), PP-binding PF00550.32 (E=8e-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_217464.1)
  • Domains: Pfam-A via hmmscan --cut_ga — AMP-binding (PF00501.35), AMP-binding_C (PF13193.13), 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 COG0236
  • Curated reference: UniProt P9WQ61 (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 — 83 functional partner(s); context anchor Rv2949c
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_003130|Rv2948c|fadD22
MRNGNLAGLLAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQRDDLSASNMTIAGGNDGGATLRERLVALRQERQRLVVDAVCAEAAKMLGEPDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGHGRLKSAGPVNSGATGLWAIEEQLNKVEELVAVIADGEKQRVADRLRALLGTIAGSEAGLGKLIQAASTPDEIFQLIDSELGK