Rv3225c Family assigned · medium auto-curated

H37Rv Rv3225c · MTBC0 mtbc0_003434 · 474 aa · 3623158–3624582 (-) · RefSeq NP_217742.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)GCN5-like N-acetyltransferase
MTBC0 PGAP re-annotationbifunctional GNAT family N-acetyltransferase/aminoglycoside 3'-phosphotransferase/choline kinase family protein
Revised (this work)Bifunctional GNAT family N-acetyltransferase/aminoglycoside 3'-phosphotransferase/choline kinase family protein. Pfam: Acetyltransf_3 (PF13302.14), Acetyltransf_1 (PF00583.32), APH (PF01636.30).

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

Curated reference (UniProt)

UniProt O05841 TrEMBL · unreviewed · Evidence at protein level
UniProt nameBifunctional AAC/APH
EC (curated) EC 2.7.1.190
Curated functionInvolved in resistance to gentamicin, tobramycin, and kanamycin. Tobramycin and kanamycin resistance is due to the ACC activity, specified by N-terminal region. The C-terminal region is a kinase that phosphorylates several 4,6-disubstituted aminoglycosides.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category K Transcription
eggNOG descriptionPhosphotransferase enzyme family
Orthologous groupCOG1670

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 0.795 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 4 synonymous, 9 missense, 0 nonsense, 2 frameshift
Disruption 2 distinct premature-stop/frameshift site(s); most common in 0.29% of strains (414) · clonal

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
Acetyltransf_3PF13302.14 2.9e-1915–152 Acetyltransferase (GNAT) domain
Acetyltransf_1PF00583.32 1.4e-0951–152 Acetyltransferase (GNAT) family
APHPF01636.30 9.9e-43210–430 Phosphotransferase enzyme family

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

Closest characterised functional partner: pks1 (polyketide synthase), medium confidence from genomic context alone (score 660 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv2946c pks1 polyketide synthase 703 660 ctx neighborhood:543
Rv2940c mas multifunctional mycocerosic acid synthase 753 653 ctx neighborhood:544
Rv2048c pks12 polyketide synthase 753 653 ctx neighborhood:544
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 753 653 ctx neighborhood:544
Rv1527c pks5 polyketide synthase 751 650 ctx neighborhood:544
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 750 649 ctx neighborhood:544
Rv2925c rnc ribonuclease III 556 557 coexpression:542
Rv1832 gcvB glycine dehydrogenase 548 549 ctx neighborhood:544
Rv2636 O-phosphotransferase 543 525 ctx cooccurence:524
Rv3226c hyp hypothetical protein 525 524 ctx neighborhood:507
Rv2378c mbtG L-lysine N6-monooxygenase 562 522 coexpression:506
Rv0802c succinyl-CoA transferase 512 512
Rv3227 aroA 3-phosphoshikimate 1-carboxyvinyltransferase 462 462 ctx neighborhood:449
Rv1004c membrane protein 416 416
Rv3228 rsgA hyp hypothetical protein 417 415 ctx neighborhood:412

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: GCN5-like N-acetyltransferase
  • MTBC0 PGAP product: bifunctional GNAT family N-acetyltransferase/aminoglycoside 3'-phosphotransferase/choline kinase family protein
  • Pfam (hmmscan --cut_ga): Acetyltransf_3 PF13302.14 (E=3e-19), Acetyltransf_1 PF00583.32 (E=1e-09), APH PF01636.30 (E=1e-42)
  • (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_217742.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Acetyltransf_3 (PF13302.14), Acetyltransf_1 (PF00583.32), APH (PF01636.30)
  • 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 COG1670
  • Curated reference: UniProt O05841 (TrEMBL, unreviewed; 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 — 31 functional partner(s); context anchor pks1
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_003434|Rv3225c|
MRFAKLSDGLSDGIVTLSPLCLDDVDAHLAGGDERLVRWLSGMPSTRASVEAYIRHCREQWVTGGPLRSFGIRTVAETIVGTIDLRFDGEGLASGQVNVAYGLYPSWRGRGLATRAVDLVCQYAAEHGATEAVIKVEPENSASARVALRAGFAFVRRICEQDGTVFDRYERVLRAKMHADEVDIDEDLVRRLLRAQFPQWADLPIAPVRSAGTDNAMYRLGEDLAVRIPRIGWAIESLRTEQQWLPRIAAHLGVASPVPVGLGSPAEGFGWPWSVCRWVAGENPSAAEFVEPNRAVEDLADFITALRATDPMGGPPAKRGAPLGEQDAEVRAALAALDGIIDVHAATAAWESALRVPPYAGPPMWFHGDLSRFNILTAQGRLTGVIDFGLMGVGDPSVDLIIAWNLLSAPARAQFRVAVGAADDDWMRGRGRALAIALIALPYYQDTNPPLAASARYAIGEVLADFRYGARPGC