Rv0669c Resolved · high auto-curated

H37Rv Rv0669c · MTBC0 mtbc0_000708 · 637 aa · 771770–773683 (-) · RefSeq NP_215183.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)neutral ceramidase
MTBC0 PGAP re-annotationneutral ceramidase
Revised (this work)Neutral ceramidase. Pfam: Ceramidase_alk (PF04734.19), Ceramidse_alk_C (PF17048.12).

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

Curated reference (UniProt)

UniProt O06769 SwissProt · reviewed · Evidence at protein level
UniProt nameNeutral ceramidase
EC (curated) EC 3.5.1.23
Curated functionCatalyzes the cleavage of the N-acyl linkage of the ceramides (Cers) to yield sphingosine (Sph) and free fatty acid. Also catalyzes the synthesis of Cers from Sph and fatty acid. Cers containning C6-C24 fatty acids are well hydrolyzed, and Cers with mono unsaturated fatty acids are much more hydrolyzed than those with saturated fatty acids.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category S Function unknown
eggNOG descriptionNeutral/alkaline non-lysosomal ceramidase, C-terminal
Orthologous groupKOG2232
EC number EC 3.5.1.23
KEGG orthology K12349
KEGG pathways map00600, map01100, map04071
KEGG modules M00099
Gene Ontology (70) GO:0001676, GO:0003674, GO:0003824, GO:0005575, GO:0005618, GO:0005623, GO:0006066, GO:0006082, GO:0006629, GO:0006631, GO:0006633, GO:0006643 +58 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 0.955 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 5 synonymous, 14 missense, 0 nonsense, 1 frameshift
Disruption 1 distinct premature-stop/frameshift site(s); most common in 0.14% of strains (197) · 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
Ceramidase_alkPF04734.19 2.6e-1524–482 Neutral/alkaline non-lysosomal ceramidase, N-terminal
Ceramidse_alk_CPF17048.12 1.4e-37485–636 Neutral/alkaline non-lysosomal ceramidase, C-terminal

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

Closest characterised functional partner: end (endonuclease IV), medium confidence from genomic context alone (score 576 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv3332 nagA N-acetylglucosamine-6-phosphate deacetylase NagA 845 824 coexpression:687 experimental:431
Rv0670 end endonuclease IV 577 576 ctx neighborhood:558
Rv1447c zwf2 glucose-6-phosphate 1-dehydrogenase 542 499 coexpression:482
Rv1121 zwf1 glucose-6-phosphate 1-dehydrogenase 539 496 coexpression:479
Rv1547 dnaE1 DNA polymerase III subunit alpha 486 486 coexpression:482
Rv3370c dnaE2 error-prone DNA polymerase 483 483 coexpression:479
Rv0671 lpqP lipoprotein LpqP 440 440 ctx neighborhood:440
Rv2043c pncA pyrazinamidase/nicotinamidase PncA 421 421 coexpression:411
Rv1834 lipZ hydrolase 413 412 ctx cooccurence:412
Rv3068c pgmA phosphoglucomutase PgmA 475 408
Rv0957 purH bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/inosinemonophosphate cyclohydrolase 424 403
Rv0189c ilvD dihydroxy-acid dehydratase 457 396
Rv1448c tal transaldolase 464 393
Rv0408 pta phosphate acetyltransferase 406 154
Rv3432c gadB glutamate decarboxylase GadB 499 118 textmining:456

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: neutral ceramidase
  • MTBC0 PGAP product: neutral ceramidase
  • Pfam (hmmscan --cut_ga): Ceramidase_alk PF04734.19 (E=3e-152), Ceramidse_alk_C PF17048.12 (E=1e-37)
  • (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_215183.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Ceramidase_alk (PF04734.19), Ceramidse_alk_C (PF17048.12)
  • 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 KOG2232
  • Curated reference: UniProt O06769 (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 — 19 functional partner(s); context anchor end
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_000708|Rv0669c|
MLSVGRGIADITGEAADCGMLGYGKSDQRTAGIHQRLRSRAFVFRDDSQDGDARLLLIVAELPLPMQNVNEEVLRRLADLYGDTYSEQNTLITATHTHAGPGGYCGYLLYNLTTSGFRPATFAAIVDGIVESVEHAHADVAPAEVSLSHGELYGASINRSPSAFDRNPPADKAFFPKRVDPHTTLVRIDRGEATVGVIHFFATHGTSMTNRNHLISGDNKGFAAYHWERTVGGADYLAGQPDFIAAFAQTNPGDMSPNVDGPLSPEAPPDREFDNTRRTGLCQFEDAFTQLSGATPIGAGIDARFTYVDLGSVLVRGEYTPDGEERRTGRPMFGAGAMAGTDEGPGFHGFRQGRNPFWDRLSRAMYRLARPTAAAQAPKGIVMPARLPNRIHPFVQEIVPVQLVRIGRLYLIGIPGEPTIVAGLRLRRMVASIVGADLADVLCVGYTNAYIHYVTTPEEYLEQRYEGGSTLFGRWELCALMQTVAELAEAMRDGRPVTLGRRPRPTRELSWVRGAPADAGSFGAVIAEPSATYRPGQAVEAVFVSALPNNDLRRGGTYLEVVRREGASWVRIADDGDWATSFRWQRQGRAGSHVSIRWDVPGDTTPGQYRIVHHGTARDRNGMLTAFSATTREFTVV