suhB Resolved · high auto-curated

H37Rv Rv2701c · MTBC0 mtbc0_002875 · 290 aa · 3038278–3039150 (-) · RefSeq NP_217217.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)inositol-1-monophosphatase SuhB
MTBC0 PGAP re-annotationinositol-1-monophosphatase SuhB
Revised (this work)Inositol-1-monophosphatase SuhB. Pfam: Inositol_P (PF00459.31).

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

Curated reference (UniProt)

UniProt P9WKI9 SwissProt · reviewed · Evidence at protein level
UniProt nameInositol-1-monophosphatase SuhB
EC (curated) EC 3.1.3.25
Curated functionCatalyzes the dephosphorylation of inositol 1-phosphate (I-1-P) to yield free myo-inositol, a key metabolite in mycobacteria. Is also able to hydrolyze a variety of polyol phosphates such as glucitol-6-phosphate, inositol 2-phosphate (I-2-P), glycerol-2-phosphate, and 2'-AMP, albeit with reduced efficiency.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category G Carbohydrate transport and metabolism
Preferred namesuhB
eggNOG descriptionInositol monophosphatase
Orthologous groupCOG0483
EC number EC 3.1.3.25
KEGG orthology K01092
KEGG pathways map00521, map00562, map01100, map04070
KEGG modules M00131
Gene Ontology (50) GO:0000287, GO:0003674, GO:0003824, GO:0005488, GO:0005975, GO:0006020, GO:0006066, GO:0006793, GO:0006796, GO:0007154, GO:0007165, GO:0008150 +38 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 1.133 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 1 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
Inositol_PPF00459.31 2.5e-6810–281 Inositol monophosphatase family

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

Closest characterised functional partner: ppgK (polyphosphate glucokinase), medium confidence from genomic context alone (score 628 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1604 impA inositol-monophosphatase ImpA 939 929 database:900
Rv0046c ino1 inositol-3-phosphate synthase 959 908 database:900 textmining:582
Rv2351c plcA membrane-associated phospholipase A 900 901 database:900
Rv1755c plcD Rv1755c, (MT1799, MTCY28.21c), len: 280 aa. Probable plcD, phospholipase C 4 (fragment) (see citations below),highly similar to C-terminus o 900 900 database:900
Rv2349c plcC phospholipase C 900 900 database:900
Rv2350c plcB membrane-associated phospholipase B 900 900 database:900
Rv2702 ppgK polyphosphate glucokinase 628 628 ctx neighborhood:626
Rv2841c nusA transcription termination/antitermination protein NusA 564 563 experimental:484
Rv1407 fmu 16S rRNA m5C967 methyltransferase 633 507 experimental:405
Rv1390 rpoZ DNA-directed RNA polymerase subunit omega 505 506 experimental:484
Rv0668 rpoC DNA-directed RNA polymerase subunit beta' 492 487 experimental:484
Rv0667 rpoB DNA-directed RNA polymerase subunit beta 485 486 experimental:484
Rv0639 nusG transcription termination/antitermination protein NusG 522 471 experimental:449
Rv3859c gltB glutamate synthase large subunit 492 463 ctx neighborhood:463
Rv2533c nusB N utilization substance protein B 494 462 experimental:405

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: inositol-1-monophosphatase SuhB
  • MTBC0 PGAP product: inositol-1-monophosphatase SuhB
  • Pfam (hmmscan --cut_ga): Inositol_P PF00459.31 (E=2e-68)
  • (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_217217.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Inositol_P (PF00459.31)
  • 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 COG0483
  • Curated reference: UniProt P9WKI9 (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 — 29 functional partner(s); context anchor ppgK
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_002875|Rv2701c|suhB
MTRPDNEPARLRSVAENLAAEAAAFVRGRRAEVFGISRAGDGDGAVRAKSSPTDPVTVVDTDTERLLRDRLAQLRPGDPILGEEGGGPADVTATPSDRVTWVLDPIDGTVNFVYGIPAYAVSIGAQVGGITVAGAVADVAARTVYSAATGLGAHLTDERGRHVLRCTGVDELSMALLGTGFGYSVRCREKQAELLAHVVPLVRDVRRIGSAALDLCMVAAGRLDAYYEHGVQVWDCAAGALIAAEAGARVLLSTPRAGGAGLVVVAAAPGIADELLAALQRFNGLEPIPD