proA Resolved · high auto-curated

H37Rv Rv2427c · MTBC0 mtbc0_002584 · 415 aa · 2748478–2749725 (-) · RefSeq NP_216943.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)gamma-glutamyl phosphate reductase
MTBC0 PGAP re-annotationglutamate-5-semialdehyde dehydrogenase
Revised (this work)Glutamate-5-semialdehyde dehydrogenase. Pfam: Aldedh (PF00171.28).

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

Curated reference (UniProt)

UniProt P9WHV1 SwissProt · reviewed · Evidence at protein level
UniProt nameGamma-glutamyl phosphate reductase
EC (curated) EC 1.2.1.41
Curated functionCatalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category E Amino acid transport and metabolism
Preferred nameproA
eggNOG descriptionCatalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5- carboxylate
Orthologous groupCOG0014
EC number EC 1.2.1.41
KEGG orthology K00147
KEGG pathways map00330, map00332, map01100, map01110, map01130, map01230
KEGG modules M00015
Gene Ontology (20) GO:0003674, GO:0003824, GO:0004350, GO:0005575, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0005886, GO:0008150, GO:0008152, GO:0016020 +8 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 0.282 · purifying
Polymorphic sites (≥ 0.1% of strains) 4 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
AldedhPF00171.28 2.5e-1312–302 Aldehyde dehydrogenase family

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

Closest characterised functional partner: proB (glutamate 5-kinase protein), high confidence from genomic context alone (score 1000 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv2439c proB glutamate 5-kinase protein 999 1000 ctx fusion:900 cooccurence:774 coexpression:806 database:900 textmining:705
Rv1187 rocA pyrroline-5-carboxylate dehydrogenase RocA 907 901 database:900
Rv0788 purQ phosphoribosylformylglycinamidine synthase 869 851 database:800
Rv1308 atpA ATP synthase subunit alpha 850 841 ctx fusion:840
Rv2426c hyp hypothetical protein 826 826 ctx neighborhood:817
Rv3432c gadB glutamate decarboxylase GadB 831 823 database:800
Rv2425c hyp hypothetical protein 822 822 ctx neighborhood:817
Rv3859c gltB glutamate synthase large subunit 917 807 database:800 textmining:591
Rv2860c glnA4 glutamine synthetase 910 807 database:800 textmining:556
Rv2222c glnA2 glutamine synthetase 911 806 database:800 textmining:561
Rv3858c gltD glutamate synthase small subunit 815 806 database:800
Rv2220 glnA1 glutamine synthetase 867 805 database:800
Rv1878 glnA3 glutamine synthetase GlnA 895 804 database:800 textmining:488
Rv0500 proC pyrroline-5-carboxylate reductase 936 802 ctx cooccurence:676 textmining:695
Rv2476c gdh NAD-dependent glutamate dehydrogenase 801 802 database:800

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: gamma-glutamyl phosphate reductase
  • MTBC0 PGAP product: glutamate-5-semialdehyde dehydrogenase
  • Pfam (hmmscan --cut_ga): Aldedh PF00171.28 (E=2e-13)
  • (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_216943.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Aldedh (PF00171.28)
  • 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 COG0014
  • Curated reference: UniProt P9WHV1 (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 — 51 functional partner(s); context anchor proB
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_002584|Rv2427c|proA
MTVPAPSQLDLRQEVHDAARRARVAARRLASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREADTPAAMLDRLSLNPQRVDGIAAGLRQVAGLRDPVGEVLRGYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALVGLELPADAVQLLSAADRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSVCNAAETLLVDAAIAETALPRLLAALQHAGVTVHLDPDEADLRREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARGPMGLPELTSTKWIAWGAGHTRPA