ansA Resolved · high auto-curated

H37Rv Rv1538c · MTBC0 mtbc0_001645 · 326 aa · 1751021–1752001 (-) · RefSeq NP_216054.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)L-aparaginase
MTBC0 PGAP re-annotationasparaginase
Revised (this work)Asparaginase. Pfam: Asparaginase (PF00710.26), Asparaginase_C (PF17763.7).

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

Curated reference (UniProt)

UniProt P9WPX5 SwissProt · reviewed · Evidence at protein level
UniProt nameL-asparaginase
EC (curated) EC 3.5.1.1
Curated functionHas a dual function in both nitrogen assimilation and in protection against acid stress during infection through asparagine hydrolysis and NH4(+) release. Catalyzes asparagine hydrolysis. Cannot use glutamine. Required for intracellular survival inside macrophages during host colonization. Mediates phagosome acidification arrest and resistance to acid stress through the formation of acid-neutralizing NH4(+) ions. In addition, may induce stress to primary immune cells and compromise the host immune response.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category E Amino acid transport and metabolism
J Translation, ribosomal structure and biogenesis
Preferred nameansA
eggNOG descriptionAsparaginase
Orthologous groupCOG0252
EC number EC 3.5.1.1
KEGG orthology K01424
KEGG pathways map00250, map00460, map01100, map01110
Gene Ontology (47) GO:0003674, GO:0003824, GO:0004067, GO:0005575, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0006082, GO:0006520, GO:0006528, GO:0006530 +35 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 1.155 · 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
AsparaginasePF00710.26 1.1e-4514–179 Asparaginase, N-terminal
Asparaginase_CPF17763.7 1.6e-19210–318 Glutaminase/Asparaginase C-terminal domain

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

Closest characterised functional partner: Rv1540 (RNA pseudouridine synthase), high confidence from genomic context alone (score 790 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1658 argG argininosuccinate synthase 924 907 database:900
Rv1595 nadB L-aspartate oxidase 918 905 database:900
Rv1380 pyrB aspartate carbamoyltransferase 906 902 database:900
Rv2201 asnB asparagine synthetase 914 901 database:900
Rv0357c purA adenylosuccinate synthetase 900 901 database:900
Rv3432c gadB glutamate decarboxylase GadB 935 806 database:800 textmining:682
Rv3601c panD aspartate 1-decarboxylase 875 802 database:800
Rv3709c ask aspartokinase 867 802 database:800
Rv1540 RNA pseudouridine synthase 789 790 ctx neighborhood:788
Rv1539 lspA lipoprotein signal peptidase 809 789 ctx neighborhood:788
Rv3396c guaA GMP synthase 552 553
Rv0640 rplK 50S ribosomal protein L11 409 410 coexpression:410
Rv3565 aspB aspartate aminotransferase AspB 845 187 textmining:818
Rv2903c lepB signal peptidase 552 127 textmining:508
Rv0337c aspC aspartate aminotransferase 586 114 textmining:552

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: L-aparaginase
  • MTBC0 PGAP product: asparaginase
  • Pfam (hmmscan --cut_ga): Asparaginase PF00710.26 (E=1e-45), Asparaginase_C PF17763.7 (E=2e-19)
  • (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_216054.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Asparaginase (PF00710.26), Asparaginase_C (PF17763.7)
  • 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 COG0252
  • Curated reference: UniProt P9WPX5 (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 — 19 functional partner(s); context anchor Rv1540
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001645|Rv1538c|ansA
MGANHVRNDPIMARLTVITTGGTISTTAGPDGVLRPTHCGATLIAGLDMDSDIEVVDLMALDSSKLTPADWDRIGAAVQEAFRGGADGVVITHGTDTLEETALWLDLTYAGSRPVVLTGAMLSADAPGADGPANLRDALAVAADPAARDLGVLVSFGGRVLQPLGLHKVANPDLCGFAGESLGFTSGGVRLTRTKTRPYLGDLGAAVAPRVDIVAVYPGSDAVAMDACVAAGARAVVLEALGSGNAGAAVIEGVRRHCRDGSDPVVIAVSTRVAGARVGAGYGPGHDLVEAGAVMVPRLPPSQARVLLMAALAANSPVADVIDRWG