mcr Resolved · high auto-curated

H37Rv Rv1143 · MTBC0 mtbc0_001228 · 360 aa · 1278502–1279584 (+) · RefSeq NP_215659.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)alpha-methylacyl-CoA racemase
MTBC0 PGAP re-annotationalpha-methylacyl-CoA racemase
Revised (this work)Alpha-methylacyl-CoA racemase. Pfam: CoA_transf_3 (PF02515.23).

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

Curated reference (UniProt)

UniProt O06543 SwissProt · reviewed · Evidence at protein level
UniProt nameAlpha-methylacyl-CoA racemase
EC (curated) EC 5.1.99.4
Curated functionCatalyzes the epimerization of (2R)- and (2S)-methylacyl-coenzyme A (CoA) thioesters. Accepts as substrates a wide range of alpha-methylacyl-CoAs, including (2R)-2-methylmyristoyl-CoA and (2S)-2-methylmyristoyl-CoA, (2R)-pristanoyl-CoA and (2S)-pristanoyl-CoA, and the cholesterol esters (25R)-3-oxo-cholest-4-en-26-oyl-CoA and (25S)-3-oxo-cholest-4-en-26-oyl-CoA. Can also catalyze the interconversion of the non-physiologic substrates (2R)-ibuprofenoyl-CoA and (2S)-ibuprofenoyl-CoA, which are potential competitive inhibitors of the enzyme.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category C Energy production and conversion
Preferred namemcr
eggNOG descriptioncarnitine dehydratase
Orthologous groupCOG1804
EC number EC 5.1.99.4
KEGG orthology K01796
KEGG pathways map00120, map01100, map04146
KEGG modules M00104

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 0.201 · purifying
Polymorphic sites (≥ 0.1% of strains) 5 synonymous, 3 missense, 0 nonsense, 2 frameshift
Disruption 2 distinct premature-stop/frameshift site(s); most common in 17.65% of strains (25629) · 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
CoA_transf_3PF02515.23 4.8e-815–343 CoA-transferase family III

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

Closest characterised functional partner: Rv1144 (oxidoreductase), high confidence from genomic context alone (score 906 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1144 oxidoreductase 909 906 ctx neighborhood:872
Rv0855 far fatty-acid-CoA racemase 903 903 database:900
Rv1142c echA10 enoyl-CoA hydratase EchA10 808 801 ctx neighborhood:780
Rv3504 fadE26 acyl-CoA dehydrogenase FadE26 670 658 database:631
Rv3505 fadE27 acyl-CoA dehydrogenase FadE27 669 657 database:631
Rv3515c fadD19 acyl-CoA synthetase 527 510 database:500
Rv3389c htdY 3-hydroxyacyl-thioester dehydratase HtdY 518 499
Rv0636 hadB (3R)-hydroxyacyl-ACP dehydratase subunit HadB 514 496
Rv1141c echA11 enoyl-CoA hydratase EchA11 510 491 ctx neighborhood:434
Rv1043c hyp hypothetical protein 486 486 database:482
Rv3671c marP serine protease 485 485 database:482
Rv1934c fadE17 acyl-CoA dehydrogenase FadE17 502 484
Rv1223 htrA serine protease HtrA 484 484 database:482
Rv0983 pepD serine protease PepD 483 484 database:482
Rv0125 pepA serine protease PepA 483 484 database:482

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: alpha-methylacyl-CoA racemase
  • MTBC0 PGAP product: alpha-methylacyl-CoA racemase
  • Pfam (hmmscan --cut_ga): CoA_transf_3 PF02515.23 (E=5e-81)
  • (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_215659.1)
  • Domains: Pfam-A via hmmscan --cut_ga — CoA_transf_3 (PF02515.23)
  • 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 COG1804
  • Curated reference: UniProt O06543 (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 — 37 functional partner(s); context anchor Rv1144
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001228|Rv1143|mcr
MAGPLSGLRVVELAGIGPGPHAAMILGDLGADVVRIDRPSSVDGISRDAMLRNRRIVTADLKSDQGLELALKLIAKADVLIEGYRPGVTERLGLGPEECAKVNDRLIYARMTGWGQTGPRSQQAGHDINYISLNGILHAIGRGDERPVPPLNLVGDFGGGSMFLLVGILAALWERQSSGKGQVVDAAMVDGSSVLIQMMWAMRATGMWTDTRGANMLDGGAPYYDTYECADGRYVAVGAIEPQFYAAMLAGLGLDAAELPPQNDRARWPELRALLTEAFASHDRDHWGAVFANSDACVTPVLAFGEVHNEPHIIERNTFYEANGGWQPMPAPRFSRTASSQPRPPAATIDIEAVLTDWDG