hemY Resolved · high auto-curated

H37Rv Rv2677c · MTBC0 - · 452 aa · 2992634–2993992 (-) · RefSeq YP_177675.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)protoporphyrinogen oxidase
MTBC0 PGAP re-annotation
Revised (this work)Protoporphyrinogen oxidase. Pfam: NAD_binding_8 (PF13450.13), Amino_oxidase (PF01593.31).

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

Annotated on the H37Rv protein: this gene has no 1:1 ancestral MTBC0 anchor (PE/PPE, paralogue, IS element, or otherwise unanchored CDS).

Curated reference (UniProt)

UniProt P9WMP1 SwissProt · reviewed · Evidence at protein level
UniProt nameCoproporphyrinogen III oxidase
EC (curated) EC 1.3.3.15
Curated functionInvolved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category H Coenzyme transport and metabolism
Preferred namehemG
eggNOG descriptionCatalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX
Orthologous groupCOG1232
EC number EC 1.3.3.15, EC 1.3.3.4
KEGG orthology K00231
KEGG pathways map00860, map01100, map01110
KEGG modules M00121

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 0.577 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 2 synonymous, 3 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
NAD_binding_8PF13450.13 5.4e-138–76 NAD(P)-binding Rossmann-like domain
Amino_oxidasePF01593.31 1.6e-3113–443 Flavin containing amine oxidoreductase

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

Closest characterised functional partner: hemE (uroporphyrinogen decarboxylase), high confidence from genomic context alone (score 1000 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv2678c hemE uroporphyrinogen decarboxylase 999 1000 ctx neighborhood:881 cooccurence:756 coexpression:916 database:900 textmining:535
Rv1485 hemZ ferrochelatase 997 993 ctx cooccurence:749 coexpression:712 database:900 textmining:582
Rv2850c magnesium chelatase 992 943 coexpression:436 database:900 textmining:875
Rv2676c hemQ hyp hypothetical protein 931 921 ctx neighborhood:881
Rv0958 magnesium chelatase 909 907 database:900
Rv2679 echA15 enoyl-CoA hydratase EchA15 790 791 ctx neighborhood:788
Rv3242c hyp hypothetical protein 787 788 coexpression:776
Rv2675c hyp hypothetical protein 786 786 ctx neighborhood:776
Rv2680 hyp hypothetical protein 703 703 ctx neighborhood:694
Rv2681 hyp hypothetical protein 698 698 ctx neighborhood:694
Rv0509 hemA glutamyl-tRNA reductase 737 576 ctx cooccurence:449 textmining:405
Rv0510 hemC porphobilinogen deaminase 735 534 textmining:457
Rv2393 che1 ferrochelatase 559 509 database:500
Rv0512 hemB delta-aminolevulinic acid dehydratase 690 496 textmining:411
Rv0526 thioredoxin 662 471

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

  • Annotation from H37Rv (no MTBC0 1:1 anchor; H37Rv protein used): protoporphyrinogen oxidase
  • Pfam (hmmscan --cut_ga): NAD_binding_8 PF13450.13 (E=5e-13), Amino_oxidase PF01593.31 (E=2e-31)
  • (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 YP_177675.1)
  • Domains: Pfam-A via hmmscan --cut_ga — NAD_binding_8 (PF13450.13), Amino_oxidase (PF01593.31)
  • 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 COG1232
  • Curated reference: UniProt P9WMP1 (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 — 40 functional partner(s); context anchor hemE
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>H37Rv|Rv2677c|hemY
MTPRSYCVVGGGISGLTSAYRLRQAVGDDATITLFEPADRLGGVLRTEHIGGQPMDLGAEAFVLRRPEMPALLAELGLSDRQLASTGARPLIYSQQRLHPLPPQTVVGIPSSAGSMAGLVDDATLARIDAEAARPFTWQVGSDPAVADLVADRFGDQVVARSVDPLLSGVYAGSAATIGLRAAAPSVAAALDRGATSVTDAVRQALPPGSGGPVFGALDGGYQVLLDGLVRRSRVHWVRARVVQLERGWVLRDETGGRWQADAVILAVPAPRLARLVDGIAPRTHAAARQIVSASSAVVALAVPGGTAFPHCSGVLVAGDESPHAKAITLSSRKWGQRGDVALLRLSFGRFGDEPALTASDDQLLAWAADDLVTVFGVAVDPVDVRVRRWIEAMPQYGPGHADVVAELRAGLPPTLAVAGSYLDGIGVPACVGAAGRAVTSVIEALDAQVAR