amiD Resolved · high auto-curated

H37Rv Rv3375 · MTBC0 mtbc0_003590 · 475 aa · 3815338–3816765 (+) · RefSeq NP_217892.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)amidase
MTBC0 PGAP re-annotationamidase
Revised (this work)Amidase. Pfam: Amidase (PF01425.27).

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

Curated reference (UniProt)

UniProt P9WQ93 SwissProt · reviewed · Evidence at protein level
UniProt namePutative amidase AmiD
EC (curated) EC 3.5.1.4

UniProt still lists this protein as Putative amidase AmiD; the revised annotation above is ahead of the current UniProt record.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category J Translation, ribosomal structure and biogenesis
Preferred nameamiD
eggNOG descriptionCOG0154 Asp-tRNAAsn Glu-tRNAGln amidotransferase A subunit and related amidases
Orthologous groupCOG0154
EC number EC 3.5.1.4, EC 6.3.5.6, EC 6.3.5.7
KEGG orthology K01426, K02433
KEGG pathways map00330, map00360, map00380, map00627, map00643, map00970, map01100, map01120
Gene Ontology (8) GO:0005575, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0044424, GO:0044444, GO:0044464

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 0.351 · purifying
Polymorphic sites (≥ 0.1% of strains) 6 synonymous, 6 missense, 0 nonsense, 1 frameshift
Disruption 1 distinct premature-stop/frameshift site(s); most common in 0.20% of strains (285) · 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
AmidasePF01425.27 3.3e-12138–455 Amidase

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

Closest characterised functional partner: gatB (aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B), high confidence from genomic context alone (score 969 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv3009c gatB aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B 980 969 ctx cooccurence:774 coexpression:646 experimental:629 textmining:411
Rv2922A acyP acylphosphatase 903 904 database:900
Rv3012c gatC glutamyl-tRNA(GLN) amidotransferase subunit C 913 903 coexpression:649 experimental:629
Rv3551 CoA-transferase subunit alpha 901 901 database:900
Rv3374 echA18.1 Probable enoyl-CoA hydratase EchA18.1 (Enoyl hydrase) (Unsaturated acyl-CoA hydratase) (Crotonase); Rv3374, (MTV004.32), len: 82 aa. Probabl 931 808 ctx neighborhood:799 textmining:654
Rv3373 echA18 enoyl-CoA hydratase 902 805 ctx neighborhood:799 textmining:519
Rv3293 pcd piperideine-6-carboxylic acid dehydrogenase 676 664 database:650
Rv0768 aldA aldehyde dehydrogenase AldA 673 661 database:650
Rv0223c aldehyde dehydrogenase 672 660 database:650
Rv0147 aldehyde dehydrogenase 671 659 database:650
Rv2572c aspS aspartate--tRNA ligase 727 633 experimental:405
Rv2992c gltS glutamate--tRNA ligase 697 604 experimental:549
Rv3376 phosphatase 823 541 ctx neighborhood:532 textmining:630
Rv2029c pfkB 6-phosphofructokinase PfkB 516 515 coexpression:513
Rv1379 pyrR bifunctional pyrimidine operon regulatory protein/uracil phosphoribosyltransferase 522 510 coexpression:430

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: amidase
  • MTBC0 PGAP product: amidase
  • Pfam (hmmscan --cut_ga): Amidase PF01425.27 (E=3e-121)
  • (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_217892.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Amidase (PF01425.27)
  • 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 COG0154
  • Curated reference: UniProt P9WQ93 (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 — 58 functional partner(s); context anchor gatB
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_003590|Rv3375|amiD
MTDADSAVPPRLDEDAISKLELTEVADLIRTRQLTSAEVTESTLRRIERLDPQLKSYAFVMPETALAAARAADADIARGHYEGVLHGVPIGVKDLCYTVDAPTAAGTTIFRDFRPAYDATVVARLRAAGAVIIGKLAMTEGAYLGYHPSLPTPVNPWDPTAWAGVSSSGCGVATAAGLCFGSIGSDTGGSIRFPTSMCGVTGIKPTWGRVSRHGVVELAASYDHVGPITRSAHDAAVLLSVIAGSDIHDPSCSAEPVPDYAADLALTRIPRVGVDWSQTTSFDEDTTAMLADVVKTLDDIGWPVIDVKLPALAPMVAAFGKMRAVETAIAHADTYPARADEYGPIMRAMIDAGHRLAAVEYQTLTERRLEFTRSLRRVFHDVDILLMPSAGIASPTLETMRGLGQDPELTARLAMPTAPFNVSGNPAICLPAGTTARGTPLGVQFIGREFDEHLLVRAGHAFQQVTGYHRRRPPV