glmU Resolved · high auto-curated
H37Rv Rv1018c · MTBC0 mtbc0_001093 ·
495 aa · 1143910–1145397 (-) ·
RefSeq NP_215534.1
Annotation: from legacy to revised
| Legacy (H37Rv / Mycobrowser) | bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase |
|---|---|
| MTBC0 PGAP re-annotation | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU |
| Revised (this work) | Bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU. Pfam: IspD (PF01128.26), NTP_transf_3 (PF12804.14), NTP_transferase (PF00483.30), Hexapep (PF00132.31). |
Auto-curated: this verdict and function were generated by rules from PGAP + Pfam + Foldseek and have not been hand-reviewed.
Curated reference (UniProt)
| UniProt |
P9WMN3
SwissProt · reviewed
· Evidence at protein level
|
|---|---|
| UniProt name | Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase |
| EC (curated) |
EC 2.3.1.157, EC 2.7.7.23
|
| Curated function | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. |
Functional vocabulary (eggNOG-mapper, orthology transfer)
| COG category |
M Cell wall / membrane / envelope biogenesis
|
|---|---|
| Preferred name | glmU |
| eggNOG description | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP- GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5- monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain |
| Orthologous group | COG1207 |
| EC number |
EC 2.3.1.157, EC 2.7.7.23
|
| KEGG orthology |
K04042
|
| KEGG pathways |
map00520, map01100, map01130
|
| KEGG modules |
M00362
|
| Gene Ontology (32) |
GO:0000287, GO:0003674, GO:0003824, GO:0003977, GO:0005488, GO:0008080, GO:0008150, GO:0016407, GO:0016410, GO:0016740, GO:0016746, GO:0016747 +20 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 | 0.871 · relaxed/neutral |
|---|---|
| Polymorphic sites (≥ 0.1% of strains) | 3 synonymous, 7 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)
| Pfam | Accession | i-Evalue | Residues | Description |
|---|---|---|---|---|
IspD | PF01128.26 | 4.8e-11 | 8–225 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
NTP_transf_3 | PF12804.14 | 3.1e-18 | 9–142 | MobA-like NTP transferase domain |
NTP_transferase | PF00483.30 | 4.7e-17 | 10–231 | Nucleotidyl transferase |
Hexapep | PF00132.31 | 2.9e-06 | 277–311 | Bacterial transferase hexapeptide (six repeats) |
Functional interaction network (STRING v12, guilt-by-association)
Closest characterised functional partner: prsA (ribose-phosphate pyrophosphokinase), high confidence from genomic context alone (score 960 excluding text-mining).
| Partner | Product | Score | No text-mining | Channels (≥400) |
|---|---|---|---|---|
Rv1017c prsA |
ribose-phosphate pyrophosphokinase | 969 | 960 ctx | neighborhood:778 cooccurence:442 coexpression:700 |
Rv3441c mrsA |
phosphoglucosamine mutase | 993 | 948 ctx | cooccurence:465 database:900 textmining:879 |
Rv1315 murA |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase | 977 | 921 | database:900 textmining:730 |
Rv0408 pta |
phosphate acetyltransferase | 968 | 838 | experimental:810 textmining:812 |
Rv3436c glmS |
glucosamine--fructose-6-phosphate aminotransferase | 962 | 823 ctx | fusion:590 coexpression:464 textmining:798 |
Rv2158c murE |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase | 926 | 773 ctx | fusion:748 textmining:692 |
Rv1016c lpqT |
lipoprotein LpqT | 748 | 749 ctx | neighborhood:747 |
Rv1302 rfe |
decaprenyl-phosphate N-acetylglucosaminephosphotransferase | 647 | 608 | database:500 |
Rv1307 atpH |
ATP synthase subunit b/delta | 569 | 554 | coexpression:414 |
Rv3859c gltB |
glutamate synthase large subunit | 545 | 545 ctx | neighborhood:544 |
Rv2883c pyrH |
uridylate kinase | 578 | 508 | |
Rv1019 |
transcriptional regulator | 492 | 492 ctx | neighborhood:492 |
Rv1020 mfd |
transcription-repair coupling factor | 514 | 490 ctx | neighborhood:486 |
Rv2152c murC |
UDP-N-acetylmuramate--alanine ligase | 871 | 487 ctx | fusion:441 textmining:760 |
Rv2845c proS |
proline--tRNA ligase | 486 | 487 ctx | cooccurence:439 |
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: bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
- MTBC0 PGAP product: bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
- Pfam (hmmscan --cut_ga): IspD PF01128.26 (E=5e-11), NTP_transf_3 PF12804.14 (E=3e-18), NTP_transferase PF00483.30 (E=5e-17), Hexapep PF00132.31 (E=3e-06)
- (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_215534.1)
- Domains: Pfam-A via hmmscan --cut_ga — IspD (PF01128.26), NTP_transf_3 (PF12804.14), NTP_transferase (PF00483.30), Hexapep (PF00132.31)
- 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
COG1207 - Curated reference: UniProt P9WMN3 (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 —
60 functional partner(s); context anchor
prsA - Primary literature: none located yet; annotation rests on the domain/homology sources above.
Ancestral MTBC0 protein sequence
>mtbc0_001093|Rv1018c|glmU MTFPGDTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLGRTIDVALQDRPLGTGHAVLCGLSALPDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVEQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLAELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVRTHGSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKRPGSPAAQASKRASEMACQQPTQPPDADQTP