Rv1692 Family assigned · medium auto-curated

H37Rv Rv1692 · MTBC0 mtbc0_001800 · 353 aa · 1928713–1929774 (+) · RefSeq NP_216208.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)phosphatase
MTBC0 PGAP re-annotationHAD-IIA family hydrolase
Revised (this work)HAD-IIA family hydrolase. Pfam: Hydrolase (PF00702.33), Hydrolase_6 (PF13344.13), Hydrolase_like (PF13242.13), GNAT_like (PF18407.8).

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

Curated reference (UniProt)

UniProt O33194 SwissProt · reviewed · Evidence at protein level
UniProt nameD-glycerol 3-phosphate phosphatase
Curated functionDephosphorylates D-glycerol 3-phosphate (sn-glycerol 1-phosphate). Is the final enzyme involved in the recycling/catabolism of glycerophospholipid polar heads. To a lesser extent, is also able to act on glycerol 2-phosphate and D-ribulose 5-phosphate, but cannot use D-glyceraldehyde 3-phosphate, dihydroxyacetone-phosphate, UMP or GMP as substrates.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category G Carbohydrate transport and metabolism
Preferred nameyutF
eggNOG descriptionhydrolase
Orthologous groupCOG0647
Gene Ontology (43) GO:0000121, GO:0000287, GO:0003674, GO:0003824, GO:0005488, GO:0005515, GO:0006629, GO:0006644, GO:0006650, GO:0006793, GO:0006796, GO:0008150 +31 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 0.358 · purifying
Polymorphic sites (≥ 0.1% of strains) 4 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
HydrolasePF00702.33 1.3e-109–222 haloacid dehalogenase-like hydrolase
Hydrolase_6PF13344.13 2.7e-2012–108 Haloacid dehalogenase-like hydrolase
Hydrolase_likePF13242.13 2.9e-17183–256 HAD-hyrolase-like
GNAT_likePF18407.8 1.5e-17269–340 GCN5-related N-acetyltransferase like domain

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

Closest characterised functional partner: ppnK (inorganic polyphosphate/ATP-NAD kinase), high confidence from genomic context alone (score 882 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1691 hyp hypothetical protein 996 976 ctx neighborhood:882 fusion:795 textmining:876
Rv3696c glpK glycerol kinase 913 905 database:900
Rv1551 plsB1 acyltransferase PlsB 900 901 database:900
Rv2482c plsB2 glycerol-3-phosphate acyltransferase 900 901 database:900
Rv3045 adhC NADP-dependent alcohol dehydrogenase 900 900 database:900
Rv1695 ppnK inorganic polyphosphate/ATP-NAD kinase 984 882 ctx neighborhood:882 textmining:870
Rv1693 hyp hypothetical protein 984 882 ctx neighborhood:882 textmining:870
Rv1694 tlyA 16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA 944 882 ctx neighborhood:882 textmining:548
Rv1696 recN DNA repair protein RecN 980 867 ctx neighborhood:867 textmining:861
Rv1690 lprJ lipoprotein LprJ 741 741 ctx neighborhood:741
Rv1697 steA hyp hypothetical protein 606 606 ctx neighborhood:606
Rv1698 mctB copper transporter MctB 573 574 ctx neighborhood:574
Rv1712 cmk cytidylate kinase 468 469
Rv1700 NUDIX hydrolase 485 464 ctx neighborhood:451
Rv1699 pyrG CTP synthase 471 451 ctx neighborhood:451

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: phosphatase
  • MTBC0 PGAP product: HAD-IIA family hydrolase
  • Pfam (hmmscan --cut_ga): Hydrolase PF00702.33 (E=1e-10), Hydrolase_6 PF13344.13 (E=3e-20), Hydrolase_like PF13242.13 (E=3e-17), GNAT_like PF18407.8 (E=2e-17)
  • (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_216208.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Hydrolase (PF00702.33), Hydrolase_6 (PF13344.13), Hydrolase_like (PF13242.13), GNAT_like (PF18407.8)
  • 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 COG0647
  • Curated reference: UniProt O33194 (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 — 20 functional partner(s); context anchor ppnK
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001800|Rv1692|
MKSIAQEHDCLLIDLDGTVFCGRQPTGGAVQSLSQVRSRKLFVTNNASRSADEVAAHLCELGFTATGEDVVTSAQSAAHLLAGQLAPGARVLIVGTEALANEVAAVGLRPVRRFEDRPDAVVQGLSMTTGWSDLAEAALAIRAGALWVAANVDPTLPTERGLLPGNGSMVAALRTATGMDPRVAGKPAPALMTEAVARGDFRAALVVGDRLDTDIEGANAAGLPSLMVLTGVNSAWDAVYAEPVRRPTYIGHDLRSLHQDSKLLAVAPQPGWQIDVGGGAVTVCANGDVDDLEFIDDGLSIVRAVASAVWEARAADLHQRPLRIEAGDERARAALQRWSLMRSDHPVTSVGTQ