thiD Resolved · high auto-curated

H37Rv Rv0422c · MTBC0 - · 265 aa · 507758–508555 (-) · RefSeq NP_214936.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
MTBC0 PGAP re-annotation
Revised (this work)Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase. Pfam: Phos_pyr_kin (PF08543.18), PfkB (PF00294.30).

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 P9WG77 SwissProt · reviewed · Evidence at protein level
UniProt nameHydroxymethylpyrimidine/phosphomethylpyrimidine kinase
EC (curated) EC 2.7.1.49, EC 2.7.4.7
Curated functionCatalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category H Coenzyme transport and metabolism
Preferred namethiD
eggNOG descriptionPhosphomethylpyrimidine kinase
Orthologous groupCOG0351
EC number EC 2.7.1.49, EC 2.7.4.7
KEGG orthology K00941
KEGG pathways map00730, map01100
KEGG modules M00127
Gene Ontology (2) GO:0008150, GO:0040007

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 0.149 · strong purifying
Polymorphic sites (≥ 0.1% of strains) 5 synonymous, 2 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
Phos_pyr_kinPF08543.18 7.4e-8613–258 Phosphomethylpyrimidine kinase
PfkBPF00294.30 3.3e-10115–238 pfkB family carbohydrate kinase

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

Closest characterised functional partner: thiE (thiamine-phosphate synthase), high confidence from genomic context alone (score 999 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0414c thiE thiamine-phosphate synthase 999 999 ctx fusion:895 cooccurence:765 coexpression:742 database:900 textmining:595
Rv0423c thiC phosphomethylpyrimidine synthase 998 997 ctx neighborhood:846 coexpression:806 database:900
Rv0421c hyp hypothetical protein 970 971 ctx neighborhood:882 coexpression:761
Rv0417 thiG thiazole synthase 957 853 ctx cooccurence:422 coexpression:715 textmining:725
Rv0416 thiS sulfur carrier protein ThiS 812 813 coexpression:781
Rv3211 rhlE ATP-dependent RNA helicase RhlE 569 568 ctx fusion:492
Rv2338c moeW molybdopterin biosynthesis protein MoeW 584 550 coexpression:428
Rv3859c gltB glutamate synthase large subunit 542 542 ctx neighborhood:538
Rv3455c truA tRNA pseudouridine synthase A 539 539 coexpression:501
Rv1253 deaD ATP-dependent RNA helicase DeaD 525 525 ctx fusion:447
Rv0427c xthA exodeoxyribonuclease III protein XthA 517 517
Rv1355c moeY molybdopterin biosynthesis protein MoeY 552 516 coexpression:430
Rv3206c moeB1 adenylyltransferase/sulfurtransferase MoeZ 633 501 coexpression:433
Rv3116 moeB2 molybdenum cofactor biosynthesis protein MoeB 631 498 coexpression:430
Rv0420c transmembrane protein 489 489 ctx neighborhood:486

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): hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
  • Pfam (hmmscan --cut_ga): Phos_pyr_kin PF08543.18 (E=7e-86), PfkB PF00294.30 (E=3e-10)
  • (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_214936.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Phos_pyr_kin (PF08543.18), PfkB (PF00294.30)
  • 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 COG0351
  • Curated reference: UniProt P9WG77 (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 — 43 functional partner(s); context anchor thiE
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>H37Rv|Rv0422c|thiD
MTPPRVLSIAGSDSGGGAGIQADMRTMALLGVHACVAVTAVTVQNTLGVKDIHEVPNDVVAGQIEAVVTDIGVQAAKTGMLASSRIVATVAATWRRLELSVPLVVDPVCASMHGDPLLAPSALDSLRGQLFPLATLLTPNLDEARLLVDIEVVDAESQRAAAKALHALGPQWVLVKGGHLRSSDGSCDLLYDGVSCYQFDAQRLPTGDDHGGGDTLATAIAAALAHGFTVPDAVDFGKRWVTECLRAAYPLGRGHGPVSPLFRLS