nudC Resolved · high auto-curated

H37Rv Rv3199c · MTBC0 mtbc0_003403 · 313 aa · 3593744–3594685 (-) · RefSeq NP_217715.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)NADH pyrophosphatase
MTBC0 PGAP re-annotationNAD(+) diphosphatase
Revised (this work)NAD(+) diphosphatase. Pfam: NUDIX-like (PF09296.18), Zn_ribbon_NUD (PF09297.17), NUDIX (PF00293.35).

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

Curated reference (UniProt)

UniProt P9WIX5 SwissProt · reviewed · Inferred from homology
UniProt nameNAD-capped RNA hydrolase NudC
EC (curated) EC 3.6.1.-, EC 3.6.1.22
Curated functionmRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category L Replication, recombination and repair
Preferred namenudC
eggNOG descriptionNADH pyrophosphatase
Orthologous groupCOG2816
EC number EC 3.6.1.22
KEGG orthology K03426
KEGG pathways map00760, map01100, map04146
Gene Ontology (6) GO:0005575, GO:0005623, GO:0005886, GO:0016020, GO:0044464, GO:0071944

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 1.735 · diversifying/relaxed
Polymorphic sites (≥ 0.1% of strains) 1 synonymous, 5 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
NUDIX-likePF09296.18 4.6e-0650–134 NADH pyrophosphatase-like rudimentary NUDIX domain
Zn_ribbon_NUDPF09297.17 1.5e-09136–167 NADH pyrophosphatase zinc ribbon domain
NUDIXPF00293.35 5.7e-21172–283 NUDIX domain

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

Closest characterised functional partner: adnA (ATP-dependent DNA helicase), high confidence from genomic context alone (score 828 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1151c cobB NAD-dependent protein deacylase 941 912 database:900
Rv2438c nadE glutamine-dependent NAD(+) synthetase 939 907 database:900
Rv1901 cinA competence damage-inducible protein CinA 955 906 database:900 textmining:547
Rv1330c pncB1 nicotinic acid phosphoribosyltransferase PncB1 961 905 database:900 textmining:609
Rv0573c pncB2 nicotinic acid phosphoribosyltransferase PncB2 939 905 database:900
Rv1596 nadC nicotinate-nucleotide pyrophosphatase 943 904 database:900 textmining:433
Rv2421c nadD nicotinate-nucleotide adenylyltransferase 933 901 database:900
Rv1695 ppnK inorganic polyphosphate/ATP-NAD kinase 905 901 database:900
Rv0156 pntAb NAD(P) transhydrogenase subunit alpha PntAb 903 901 database:900
Rv0157 pntB NAD(P) transhydrogenase subunit beta PntB 900 901 database:900
Rv0155 pntAa NAD(P) transhydrogenase subunit alpha PntAa 900 901 database:900
Rv2713 sthA pyridine nucleotide transhydrogenase 910 900 database:900
Rv0212c nadR transcriptional regulator NadR 904 900 database:900
Rv3202c adnA ATP-dependent DNA helicase 828 828 ctx neighborhood:747
Rv3200c transmembrane cation transporter 810 810 ctx neighborhood:804

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: NADH pyrophosphatase
  • MTBC0 PGAP product: NAD(+) diphosphatase
  • Pfam (hmmscan --cut_ga): NUDIX-like PF09296.18 (E=5e-06), Zn_ribbon_NUD PF09297.17 (E=1e-09), NUDIX PF00293.35 (E=6e-21)
  • (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_217715.1)
  • Domains: Pfam-A via hmmscan --cut_ga — NUDIX-like (PF09296.18), Zn_ribbon_NUD (PF09297.17), NUDIX (PF00293.35)
  • 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 COG2816
  • Curated reference: UniProt P9WIX5 (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 — 29 functional partner(s); context anchor adnA
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_003403|Rv3199c|nudC
MTNVSGVDFQLRSVPLLSRVGADRADRLRTDMEAAAAGWPGAALLRVDSRNRVLVANGRVLLGAAIELADKPPPEAVFLGRVEGGRHVWAVRAALQPIADPDIPAEAVDLRGLGRIMDDTSSQLVSSASALLNWHDNARFSALDGAPTKPARAGWSRVNPITGHEEFPRIDPAVICLVHDGADRAVLARQAAWPERMFSLLAGFVEAGESFEVCVAREIREEIGLTVRDVRYLGSQPWPFPRSLMVGFHALGDPDEEFSFSDGEIAEAAWFTRDEVRAALAAGDWSSASESKLLLPGSISIARVIIESWAACE