argA Resolved · high auto-curated

H37Rv Rv2747 · MTBC0 mtbc0_002924 · 174 aa · 3081677–3082201 (+) · RefSeq NP_217263.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)L-glutamate alpha-N-acetyltranferase
MTBC0 PGAP re-annotationamino-acid N-acetyltransferase
Revised (this work)Amino-acid N-acetyltransferase. Pfam: Acetyltransf_1 (PF00583.32), Acetyltransf_7 (PF13508.14).

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

Curated reference (UniProt)

UniProt O33289 SwissProt · reviewed · Evidence at protein level
UniProt nameAmino-acid acetyltransferase
EC (curated) EC 2.3.1.1
Curated functionCatalyzes the conversion of L-glutamate to alpha-N-acetyl-L-glutamate. L-glutamine is a significantly better substrate compared to L-glutamate.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category E Amino acid transport and metabolism
Preferred nameargA
eggNOG descriptionN-acetylglutamate synthase
Orthologous groupCOG1246
EC number EC 2.3.1.1
KEGG orthology K00619
KEGG pathways map00220, map01100, map01110, map01130, map01210, map01230
KEGG modules M00028
Gene Ontology (54) GO:0003674, GO:0003824, GO:0004042, GO:0005488, GO:0005515, GO:0006082, GO:0006520, GO:0006525, GO:0006526, GO:0006591, GO:0006807, GO:0008080 +42 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 0.0 · strong purifying
Polymorphic sites (≥ 0.1% of strains) 1 synonymous, 0 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
Acetyltransf_1PF00583.32 5.7e-1349–127 Acetyltransferase (GNAT) family
Acetyltransf_7PF13508.14 5.5e-1249–129 Acetyltransferase (GNAT) domain

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

Closest characterised functional partner: pgsA3 (CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase), high confidence from genomic context alone (score 721 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1654 argB acetylglutamate kinase 960 939 database:900
Rv1653 argJ bifunctional glutamate N-acetyltransferase/amino-acid acetyltransferase 989 937 database:900 textmining:845
Rv0428c GCN5-like N-acetyltransferase 907 903 database:900
Rv0337c aspC aspartate aminotransferase 906 901 database:900
Rv2476c gdh NAD-dependent glutamate dehydrogenase 900 900 database:900
Rv2746c pgsA3 CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 721 721 ctx neighborhood:649
Rv3859c gltB glutamate synthase large subunit 734 545 ctx neighborhood:544 textmining:440
Rv1658 argG argininosuccinate synthase 629 517 coexpression:477
Rv2745c clgR transcriptional regulator ClgR 511 511 ctx neighborhood:503
Rv2169c transmembrane protein 489 490 ctx cooccurence:489
Rv0637 hadC (3R)-hydroxyacyl-ACP dehydratase subunit HadC 486 486 ctx cooccurence:483
Rv1652 argC N-acetyl-gamma-glutamyl-phoshate reductase 659 426 textmining:430
Rv0504c hyp hypothetical protein 424 424 ctx cooccurence:420
Rv0635 hadA (3R)-hydroxyacyl-ACP dehydratase subunit HadA 415 415 ctx cooccurence:412
Rv2146c transmembrane protein 415 415 ctx cooccurence:403

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-glutamate alpha-N-acetyltranferase
  • MTBC0 PGAP product: amino-acid N-acetyltransferase
  • Pfam (hmmscan --cut_ga): Acetyltransf_1 PF00583.32 (E=6e-13), Acetyltransf_7 PF13508.14 (E=6e-12)
  • (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_217263.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Acetyltransf_1 (PF00583.32), Acetyltransf_7 (PF13508.14)
  • 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 COG1246
  • Curated reference: UniProt O33289 (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 — 27 functional partner(s); context anchor pgsA3
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_002924|Rv2747|argA
MTERPRDCRPVVRRARTSDVPAIKQLVDTYAGKILLEKNLVTLYEAVQEFWVAEHPDLYGKVVGCGALHVLWSDLGEIRTVAVDPAMTGHGIGHAIVDRLLQVARDLQLQRVFVLTFETEFFARHGFTEIEGTPVTAEVFDEMCRSYDIGVAEFLDLSYVKPNILGNSRMLLVL