UniProtKB - P9WMN3 (GLMU_MYCTU)
Protein
Bifunctional protein GlmU
Gene
glmU
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
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.UniRule annotation2 Publications
Catalytic activityi
- acetyl-CoA + α-D-glucosamine 1-phosphate = CoA + H+ + N-acetyl-α-D-glucosamine 1-phosphateUniRule annotation2 PublicationsEC:2.3.1.157UniRule annotation2 Publications
- H+ + N-acetyl-α-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-α-D-glucosamineUniRule annotation2 PublicationsEC:2.7.7.23UniRule annotation2 Publications
Cofactori
Mg2+5 Publications, Co2+2 PublicationsNote: Binds 1 Mg2+ ion per subunit (PubMed:19237750, PubMed:19121323, Ref.7, Ref.8, PubMed:23485416). Can also use Co2+ ion to a lesser extent (Ref.8) (PubMed:23485416).5 Publications
Kineticsi
- KM=106.75 µM for GlcNAc-1-P (at pH 7.6)1 Publication
- KM=61.86 µM for UTP (at pH 7.6)1 Publication
- KM=240 µM for GlcN-1-P (at pH 7.6)1 Publication
- KM=304 µM for acetyl-CoA (at pH 7.6)1 Publication
- Vmax=1.869 µmol/min/mg enzyme (Uridyltransferase activity) (at pH 7.6)1 Publication
- Vmax=4.489 µmol/min/mg enzyme (Acetyltransferase activity) (at pH 7.6)1 Publication
: UDP-N-acetyl-alpha-D-glucosamine biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II).UniRule annotationProteins known to be involved in the 2 steps of the subpathway in this organism are:
- no protein annotated in this organism
- Bifunctional protein GlmU (glmU)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.
Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis
This protein is involved in step 1 of the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotationProteins known to be involved in this subpathway in this organism are:
- Bifunctional protein GlmU (glmU)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.
Pathwayi: LPS lipid A biosynthesis
This protein is involved in the pathway LPS lipid A biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotationView all proteins of this organism that are known to be involved in the pathway LPS lipid A biosynthesis and in Bacterial outer membrane biogenesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 26 | UDP-GlcNAcUniRule annotation1 Publication | 1 | |
Binding sitei | 83 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Metal bindingi | 114 | Magnesium or cobalt4 Publications | 1 | |
Binding sitei | 151 | UDP-GlcNAc; via amide nitrogenUniRule annotation4 Publications | 1 | |
Binding sitei | 166 | UDP-GlcNAcUniRule annotation4 Publications | 1 | |
Binding sitei | 181 | UDP-GlcNAcUniRule annotation4 Publications | 1 | |
Metal bindingi | 239 | Magnesium or cobalt4 Publications | 1 | |
Binding sitei | 239 | UDP-GlcNAcUniRule annotation4 Publications | 1 | |
Binding sitei | 344 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Binding sitei | 362 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Active sitei | 374 | Proton acceptorUniRule annotation1 Publication | 1 | |
Binding sitei | 377 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Binding sitei | 388 | UDP-GlcNAcUniRule annotation1 Publication | 1 | |
Binding sitei | 391 | Acetyl-CoA; via amide nitrogenUniRule annotation1 Publication | 1 | |
Binding sitei | 416 | Acetyl-CoA; via carbonyl oxygenUniRule annotation1 Publication | 1 | |
Binding sitei | 434 | Acetyl-CoA; via amide nitrogen1 Publication | 1 |
GO - Molecular functioni
- glucosamine-1-phosphate N-acetyltransferase activity Source: MTBBASE
- magnesium ion binding Source: MTBBASE
- UDP-N-acetylglucosamine diphosphorylase activity Source: MTBBASE
- uridylyltransferase activity Source: MTBBASE
GO - Biological processi
- adhesion of symbiont to host cell Source: AgBase
- cell morphogenesis Source: UniProtKB-UniRule
- cell wall organization Source: UniProtKB-KW
- entry of bacterium into host cell Source: AgBase
- lipid A biosynthetic process Source: UniProtKB-UniPathway
- lipopolysaccharide biosynthetic process Source: InterPro
- peptidoglycan biosynthetic process Source: UniProtKB-UniRule
- regulation of cell shape Source: UniProtKB-KW
- UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Acyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Transferase |
Biological process | Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
SABIO-RKi | P9WMN3 |
UniPathwayi | UPA00113;UER00532 UPA00113;UER00533 UPA00973 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional protein GlmUUniRule annotationIncluding the following 2 domains: UDP-N-acetylglucosamine pyrophosphorylaseUniRule annotation (EC:2.7.7.23UniRule annotation2 Publications) Alternative name(s): N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation2 Publications) |
Gene namesi | Name:glmUUniRule annotation Ordered Locus Names:Rv1018c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv1018c |
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000233802 | 2 – 495 | Bifunctional protein GlmUAdd BLAST | 494 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylthreonineCombined sources | 1 | |
Cross-linki | 362 | Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication |
Post-translational modificationi
Phosphorylated at the C-terminal domain by PknB. The phosphorylation is required for acetyltransferase activity, but does not affect uridyltransferase activity.1 Publication
Keywords - PTMi
Acetylation, Isopeptide bond, Ubl conjugationProteomic databases
PaxDbi | P9WMN3 |
PTM databases
iPTMneti | P9WMN3 |
Interactioni
Subunit structurei
Homotrimer.
UniRule annotation4 PublicationsBinary interactionsi
P9WMN3
With | #Exp. | IntAct |
---|---|---|
CXCL8 [P10145] from Homo sapiens. | 3 | EBI-11740532,EBI-3917999 |
Protein-protein interaction databases
IntActi | P9WMN3, 1 interactor |
STRINGi | 83332.Rv1018c |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WMN3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 241 | PyrophosphorylaseUniRule annotationAdd BLAST | 240 | |
Regioni | 12 – 15 | UDP-GlcNAc bindingUniRule annotation4 Publications | 4 | |
Regioni | 88 – 89 | UDP-GlcNAc bindingUniRule annotation4 Publications | 2 | |
Regioni | 112 – 114 | UDP-GlcNAc bindingUniRule annotation3 Publications | 3 | |
Regioni | 242 – 262 | LinkerUniRule annotationAdd BLAST | 21 | |
Regioni | 263 – 495 | N-acetyltransferaseUniRule annotationAdd BLAST | 233 | |
Regioni | 397 – 398 | Acetyl-CoA bindingUniRule annotation | 2 |
Sequence similaritiesi
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.UniRule annotation
In the C-terminal section; belongs to the transferase hexapeptide repeat family.UniRule annotation
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | COG1207, Bacteria |
OMAi | TAIVEHK |
PhylomeDBi | P9WMN3 |
Family and domain databases
CDDi | cd03353, LbH_GlmU_C, 1 hit |
Gene3Di | 3.90.550.10, 1 hit |
HAMAPi | MF_01631, GlmU, 1 hit |
InterProi | View protein in InterPro IPR005882, Bifunctional_GlmU IPR038009, GlmU_C_LbH IPR001451, Hexapep IPR025877, MobA-like_NTP_Trfase IPR029044, Nucleotide-diphossugar_trans IPR011004, Trimer_LpxA-like_sf |
Pfami | View protein in Pfam PF00132, Hexapep, 3 hits PF12804, NTP_transf_3, 1 hit |
SUPFAMi | SSF51161, SSF51161, 1 hit SSF53448, SSF53448, 1 hit |
TIGRFAMsi | TIGR01173, glmU, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P9WMN3-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTFPGDTAVL VLAAGPGTRM RSDTPKVLHT LAGRSMLSHV LHAIAKLAPQ
60 70 80 90 100
RLIVVLGHDH QRIAPLVGEL ADTLGRTIDV ALQDRPLGTG HAVLCGLSAL
110 120 130 140 150
PDDYAGNVVV TSGDTPLLDA DTLADLIATH RAVSAAVTVL TTTLDDPFGY
160 170 180 190 200
GRILRTQDHE VMAIVEQTDA TPSQREIREV NAGVYAFDIA ALRSALSRLS
210 220 230 240 250
SNNAQQELYL TDVIAILRSD GQTVHASHVD DSALVAGVNN RVQLAELASE
260 270 280 290 300
LNRRVVAAHQ LAGVTVVDPA TTWIDVDVTI GRDTVIHPGT QLLGRTQIGG
310 320 330 340 350
RCVVGPDTTL TDVAVGDGAS VVRTHGSSSS IGDGAAVGPF TYLRPGTALG
360 370 380 390 400
ADGKLGAFVE VKNSTIGTGT KVPHLTYVGD ADIGEYSNIG ASSVFVNYDG
410 420 430 440 450
TSKRRTTVGS HVRTGSDTMF VAPVTIGDGA YTGAGTVVRE DVPPGALAVS
460 470 480 490
AGPQRNIENW VQRKRPGSPA AQASKRASEM ACQQPTQPPD ADQTP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43768.1 |
PIRi | E70622 |
RefSeqi | NP_215534.1, NC_000962.3 WP_003405267.1, NZ_NVQJ01000018.1 |
Genome annotation databases
EnsemblBacteriai | CCP43768; CCP43768; Rv1018c |
GeneIDi | 23492850 886069 |
KEGGi | mtu:Rv1018c mtv:RVBD_1018c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43768.1 |
PIRi | E70622 |
RefSeqi | NP_215534.1, NC_000962.3 WP_003405267.1, NZ_NVQJ01000018.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2QKX | X-ray | 2.75 | A | 1-389 | [»] | |
3D8V | X-ray | 2.55 | A | 1-495 | [»] | |
3D98 | X-ray | 2.50 | A | 1-495 | [»] | |
3DJ4 | X-ray | 2.38 | A | 1-495 | [»] | |
3FOQ | X-ray | 3.41 | A | 1-495 | [»] | |
3SPT | X-ray | 2.33 | A | 1-495 | [»] | |
3ST8 | X-ray | 1.98 | A | 1-495 | [»] | |
4G3P | X-ray | 2.47 | A | 1-495 | [»] | |
4G3Q | X-ray | 1.90 | A | 1-495 | [»] | |
4G3S | X-ray | 2.04 | A | 1-495 | [»] | |
4G87 | X-ray | 2.03 | A | 1-495 | [»] | |
4HCQ | X-ray | 2.60 | A | 1-495 | [»] | |
SMRi | P9WMN3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P9WMN3, 1 interactor |
STRINGi | 83332.Rv1018c |
Chemistry databases
ChEMBLi | CHEMBL1293297 |
DrugCentrali | P9WMN3 |
PTM databases
iPTMneti | P9WMN3 |
Proteomic databases
PaxDbi | P9WMN3 |
Genome annotation databases
EnsemblBacteriai | CCP43768; CCP43768; Rv1018c |
GeneIDi | 23492850 886069 |
KEGGi | mtu:Rv1018c mtv:RVBD_1018c |
Organism-specific databases
TubercuListi | Rv1018c |
Phylogenomic databases
eggNOGi | COG1207, Bacteria |
OMAi | TAIVEHK |
PhylomeDBi | P9WMN3 |
Enzyme and pathway databases
UniPathwayi | UPA00113;UER00532 UPA00113;UER00533 UPA00973 |
SABIO-RKi | P9WMN3 |
Miscellaneous databases
PROi | PR:P9WMN3 |
Family and domain databases
CDDi | cd03353, LbH_GlmU_C, 1 hit |
Gene3Di | 3.90.550.10, 1 hit |
HAMAPi | MF_01631, GlmU, 1 hit |
InterProi | View protein in InterPro IPR005882, Bifunctional_GlmU IPR038009, GlmU_C_LbH IPR001451, Hexapep IPR025877, MobA-like_NTP_Trfase IPR029044, Nucleotide-diphossugar_trans IPR011004, Trimer_LpxA-like_sf |
Pfami | View protein in Pfam PF00132, Hexapep, 3 hits PF12804, NTP_transf_3, 1 hit |
SUPFAMi | SSF51161, SSF51161, 1 hit SSF53448, SSF53448, 1 hit |
TIGRFAMsi | TIGR01173, glmU, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GLMU_MYCTU | |
Accessioni | P9WMN3Primary (citable) accession number: P9WMN3 Secondary accession number(s): L0T872, P96382, Q7D8Z8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | December 2, 2020 | |
This is version 48 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families