purL Family assigned · medium auto-curated

H37Rv Rv0803 · MTBC0 mtbc0_000852 · 754 aa · 898887–901151 (+) · RefSeq NP_215318.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)phosphoribosylformylglycinamidine synthase 2
MTBC0 PGAP re-annotationphosphoribosylformylglycinamidine synthase subunit PurL
Revised (this work)Phosphoribosylformylglycinamidine synthase subunit PurL. Pfam: FGAR-AT_linker (PF18072.7), AIRS (PF00586.30), AIRS_C (PF02769.28).

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

Curated reference (UniProt)

UniProt P9WHL7 SwissProt · reviewed · Evidence at protein level
UniProt namePhosphoribosylformylglycinamidine synthase subunit PurL
EC (curated) EC 6.3.5.3
Curated functionPart of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to Pur.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category F Nucleotide transport and metabolism
Preferred namepurL
eggNOG descriptionPart of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL
Orthologous groupCOG0046
EC number EC 6.3.5.3
KEGG orthology K01952
KEGG pathways map00230, map01100, map01110, map01130
KEGG modules M00048
Gene Ontology (37) GO:0006139, GO:0006163, GO:0006164, GO:0006725, GO:0006753, GO:0006793, GO:0006796, GO:0006807, GO:0008150, GO:0008152, GO:0009058, GO:0009117 +25 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 0.475 · purifying
Polymorphic sites (≥ 0.1% of strains) 6 synonymous, 8 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
FGAR-AT_linkerPF18072.7 1.0e-1716–58 Formylglycinamide ribonucleotide amidotransferase linker domain
AIRSPF00586.30 3.9e-2984–198 AIR synthase related protein, N-terminal domain
AIRS_CPF02769.28 4.4e-38212–368 AIR synthase related protein, C-terminal domain

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

Closest characterised functional partner: purQ (phosphoribosylformylglycinamidine synthase), high confidence from genomic context alone (score 1000 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0788 purQ phosphoribosylformylglycinamidine synthase 999 1000 ctx fusion:899 cooccurence:774 coexpression:861 experimental:836 database:900 textmining:408
Rv0787A purS hyp hypothetical protein 999 999 ctx cooccurence:767 coexpression:858 experimental:790 database:900 textmining:417
Rv0809 purM phosphoribosylformylglycinamidine cyclo-ligase PurM 996 993 ctx cooccurence:496 coexpression:857 database:900 textmining:519
Rv0956 purN phosphoribosylglycinamide formyltransferase PurN 995 992 ctx cooccurence:443 coexpression:857 database:900 textmining:441
Rv0808 purF amidophosphoribosyltransferase 989 984 ctx fusion:624 cooccurence:577 coexpression:858
Rv0389 purT phosphoribosylglycinamide formyltransferase PurT 980 974 coexpression:731 database:900
Rv0772 purD phosphoribosylamine--glycine ligase 966 951 ctx cooccurence:467 coexpression:859
Rv3275c purE 5-(carboxyamino)imidazole ribonucleotide mutase 952 938 ctx cooccurence:547 coexpression:859
Rv3276c purK 5-(carboxyamino)imidazole ribonucleotide synthase 959 928 ctx cooccurence:473 coexpression:859 textmining:462
Rv0957 purH bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/inosinemonophosphate cyclohydrolase 951 919 coexpression:858 textmining:416
Rv0780 purC phosphoribosylaminoimidazole-succinocarboxamide synthase 921 897 coexpression:858
Rv0777 purB adenylosuccinate lyase PurB 899 869 coexpression:850
Rv3396c guaA GMP synthase 936 865 coexpression:788 textmining:554
Rv0804 hyp hypothetical protein 804 804 ctx neighborhood:801
Rv1650 pheT phenylalanine--tRNA ligase subunit beta 857 733 coexpression:670 textmining:490

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: phosphoribosylformylglycinamidine synthase 2
  • MTBC0 PGAP product: phosphoribosylformylglycinamidine synthase subunit PurL
  • Pfam (hmmscan --cut_ga): FGAR-AT_linker PF18072.7 (E=1e-17), AIRS PF00586.30 (E=4e-29), AIRS_C PF02769.28 (E=4e-38)
  • (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_215318.1)
  • Domains: Pfam-A via hmmscan --cut_ga — FGAR-AT_linker (PF18072.7), AIRS (PF00586.30), AIRS_C (PF02769.28)
  • 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 COG0046
  • Curated reference: UniProt P9WHL7 (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 — 57 functional partner(s); context anchor purQ
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_000852|Rv0803|purL
MLDTVEHAATTPDQPQPYGELGLKDDEYRRIRQILGRRPTDTELAMYSVMWSEHCSYKSSKVHLRYFGETTSDEMRAAMLAGIGENAGVVDIGDGWAVTFKVESHNHPSYVEPYQGAATGVGGIVRDIMAMGARPVAVMDQLRFGAADAPDTRRVLDGVVRGIGGYGNSLGLPNIGGETVFDPCYAGNPLVNALCVGVLRQEDLHLAFASGAGNKIILFGARTGLDGIGGVSVLASDTFDAEGSRKKLPSVQVGDPFMEKVLIECCLELYAGGLVIGIQDLGGAGLSCATSELASAGDGGMTIQLDSVPLRAKEMTPAEVLCSESQERMCAVVSPKNVDAFLAVCRKWEVLATVIGEVTDGDRLQITWHGETVVDVPPRTVAHEGPVYQRPVARPDTQDALNADRSAKLSRPVTGDELRATLLALLGSPHLCSRAFITEQYDRYVRGNTVLAEHADGGMLRIDESTGRGIAVSTDASGRYTLLDPYAGAQLALAEAYRNVAVTGATPVAVTNCLNFGSPEDPGVMWQFTQAVRGLADGCADLGIPVTGGNVSFYNQTGSAAILPTPVVGVLGVIDDVRRRIPTGLGAEPGETLMLLGDTRDEFDGSVWAQVTADHLGGLPPVVDLAREKLLAAVLSSASRDGLVSAAHDLSEGGLAQAIVESALAGETGCRIVLPEGADPFVLLFSESAGRVLVAVPRTEESRFRGMCEARGLPAVRIGVVDQGSDAVEVQGLFAVSLAELRATSEAVLPRYFG