ctaB Resolved · high auto-curated

H37Rv Rv1451 · MTBC0 mtbc0_001553 · 308 aa · 1644631–1645557 (+) · RefSeq NP_215967.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)protoheme IX farnesyltransferase
MTBC0 PGAP re-annotationheme o synthase
Revised (this work)Heme o synthase. Pfam: UbiA (PF01040.24).

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

Curated reference (UniProt)

UniProt P9WFR7 SwissProt · reviewed · Inferred from homology
UniProt nameProtoheme IX farnesyltransferase
EC (curated) EC 2.5.1.141
Curated functionConverts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category O Post-translational modification, protein turnover, chaperones
Preferred namectaB
eggNOG descriptionConverts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group
Orthologous groupCOG0109
EC number EC 2.5.1.141
KEGG orthology K02257
KEGG pathways map00190, map00860, map01100, map01110, map04714
KEGG modules M00154
Gene Ontology (47) GO:0003674, GO:0003824, GO:0004311, GO:0004659, GO:0005575, GO:0005618, GO:0005623, GO:0005886, GO:0006091, GO:0006725, GO:0006778, GO:0006779 +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 0.209 · purifying
Polymorphic sites (≥ 0.1% of strains) 7 synonymous, 4 missense, 0 nonsense, 0 frameshift

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
UbiAPF01040.24 2.4e-6035–282 UbiA prenyltransferase family

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

Closest characterised functional partner: ctaD (cytochrome C oxidase cytochrome 1), high confidence from genomic context alone (score 997 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv3043c ctaD cytochrome C oxidase cytochrome 1 999 997 ctx cooccurence:773 coexpression:820 database:900 textmining:928
Rv2193 ctaE cytochrome C oxidase subunit III 999 997 ctx cooccurence:773 coexpression:851 database:900 textmining:940
Rv2200c ctaC cytochrome C oxidase subunit II 999 994 ctx cooccurence:770 coexpression:751 database:900 textmining:853
Rv1456c antibiotic ABC transporter permease 996 990 ctx cooccurence:440 coexpression:664 experimental:471 database:900 textmining:646
Rv1485 hemZ ferrochelatase 927 906 database:900
Rv2196 qcrB ubiquinol-cytochrome C reductase cytochrome subunit B 863 677 ctx cooccurence:618 textmining:595
Rv2235 transmembrane protein 750 674 coexpression:423
Rv1448c tal transaldolase 630 607 ctx neighborhood:544
Rv1449c tkt transketolase 587 561 ctx neighborhood:544
Rv1447c zwf2 glucose-6-phosphate 1-dehydrogenase 563 536 ctx neighborhood:533
Rv1248c kgd multifunctional 2-oxoglutarate dehydrogenase E1 component /2-oxoglutarate dehydrogenase dihydrolipoyllysine-residue succinyltransferase 669 531 coexpression:467
Rv1444c hyp hypothetical protein 523 523 ctx neighborhood:523
Rv3339c icd1 isocitrate dehydrogenase 538 512 coexpression:512
Rv2195 qcrA ubiquinol-cytochrome C reductase rieske iron-sulfur subunit 658 508 ctx cooccurence:430
Rv2194 qcrC ubiquinol-cytochrome C reductase cytochrome subunit C 724 491 ctx cooccurence:423 textmining:480

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: protoheme IX farnesyltransferase
  • MTBC0 PGAP product: heme o synthase
  • Pfam (hmmscan --cut_ga): UbiA PF01040.24 (E=2e-60)
  • (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_215967.1)
  • Domains: Pfam-A via hmmscan --cut_ga — UbiA (PF01040.24)
  • 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 COG0109
  • Curated reference: UniProt P9WFR7 (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 — 46 functional partner(s); context anchor ctaD
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001553|Rv1451|ctaB
MNVRGRVAPRRVTGRAMSTLLAYLALTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNALALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMFAIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLALATSWLYGAVALVAGGWFLTMAHQLYAGVRAGEPVRPLRLFLQSNNYLAVVFCALAVDSVIALPTLH