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UniProtKB - P0ACC7 (GLMU_ECOLI)
Protein
Bifunctional protein GlmU
Gene
glmU
Organism
Escherichia coli (strain K12)
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 annotation5 PublicationsCatalytic activityi
- acetyl-CoA + α-D-glucosamine 1-phosphate = CoA + H+ + N-acetyl-α-D-glucosamine 1-phosphateUniRule annotation3 PublicationsEC:2.3.1.157UniRule annotation3 Publications
- H+ + N-acetyl-α-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-α-D-glucosamineUniRule annotation3 PublicationsEC:2.7.7.23UniRule annotation3 Publications
Cofactori
Mg2+1 Publication, Co2+1 PublicationNote: Binds 1 Mg2+ ion per subunit (PubMed:17473010). Can also use Co2+ ion to a lesser extent (PubMed:11329257).2 Publications
Activity regulationi
Inhibited by its reaction product N-acetylglucosamine-1-phosphate and by UDP-N-acetylmuramic acid, which is one of the first precursors specific for the peptidoglycan pathway.3 Publications
Kineticsi
- KM=0.018 mM for N-acetylglucosamine 1-phosphate3 Publications
- KM=0.07 mM for alpha-D-glucosamine 1-phosphate1 Publication
- KM=0.1 mM for UTP1 Publication
- KM=0.15 mM for alpha-D-glucosamine 1-phosphate3 Publications
- KM=0.25 mM for alpha-D-glucosamine 1-phosphate3 Publications
- KM=0.32 mM for acetyl-CoA3 Publications
- KM=0.6 mM for acetyl-CoA3 Publications
- KM=0.84 mM for n-propionyl-CoA3 Publications
- KM=1.3 mM for UDP-glucosamine3 Publications
- KM=2 mM for glucose-1-P3 Publications
- KM=3.7 mM for N-acetylgalactosamine-1-P3 Publications
- KM=15 mM for galactosamine-1-phosphate3 Publications
: 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 annotation This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.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 annotation This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.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 | 25 | UDP-GlcNAcUniRule annotation | 1 | |
Binding sitei | 76 | UDP-GlcNAcUniRule annotation3 Publications | 1 | |
Metal bindingi | 105 | CobaltCombined sources1 Publication | 1 | |
Metal bindingi | 105 | MagnesiumCombined sources1 Publication | 1 | |
Binding sitei | 140 | UDP-GlcNAc; via amide nitrogenUniRule annotation3 Publications | 1 | |
Binding sitei | 154 | UDP-GlcNAcUniRule annotation3 Publications | 1 | |
Binding sitei | 169 | UDP-GlcNAcUniRule annotation3 Publications | 1 | |
Metal bindingi | 227 | CobaltCombined sources1 Publication | 1 | |
Metal bindingi | 227 | MagnesiumCombined sources1 Publication | 1 | |
Binding sitei | 227 | UDP-GlcNAcUniRule annotation | 1 | |
Binding sitei | 333 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Binding sitei | 351 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Active sitei | 363 | Proton acceptorUniRule annotation | 1 | |
Binding sitei | 366 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Binding sitei | 377 | UDP-GlcNAcUniRule annotation3 Publications | 1 | |
Binding sitei | 380 | Acetyl-CoA; via amide nitrogenUniRule annotation2 Publications | 1 | |
Binding sitei | 405 | Acetyl-CoAUniRule annotation3 Publications | 1 | |
Binding sitei | 423 | Acetyl-CoA; via amide nitrogenUniRule annotation3 Publications | 1 | |
Binding sitei | 440 | Acetyl-CoAUniRule annotation3 Publications | 1 |
GO - Molecular functioni
- glucosamine-1-phosphate N-acetyltransferase activity Source: EcoCyc
- identical protein binding Source: EcoCyc
- magnesium ion binding Source: EcoCyc
- UDP-N-acetylglucosamine diphosphorylase activity Source: EcoCyc
GO - Biological processi
- cell morphogenesis Source: UniProtKB-UniRule
- cell wall organization Source: UniProtKB-KW
- lipid A biosynthetic process Source: UniProtKB-UniPathway
- peptidoglycan biosynthetic process Source: UniProtKB-UniRule
- regulation of cell shape Source: UniProtKB-KW
- UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Acyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Transferase |
Biological process | Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
Ligand | Cobalt, Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:NAG1P-URIDYLTRANS-MONOMER |
BRENDAi | 2.3.1.157, 2026 2.7.7.23, 2026 |
SABIO-RKi | P0ACC7 |
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 annotation3 Publications) Alternative name(s): N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation3 Publications) |
Gene namesi | Name:glmUUniRule annotation Synonyms:yieA Ordered Locus Names:b3730, JW3708 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation1 Publication
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 14 | G → A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP. 1 Publication | 1 | |
Mutagenesisi | 18 | R → A: Dramatically impairs the uridyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 25 | K → A: 8-fold decrease in uridyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 296 | C → A: No effect. 1 Publication | 1 | |
Mutagenesisi | 307 | C → A: 1350-fold decrease in acetyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 324 | C → A: 8-fold decrease in acetyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 385 | C → A: No effect. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3414415 |
DrugBanki | DB03814, 2-(N-morpholino)ethanesulfonic acid DB01992, Coenzyme A DB03397, Uridine-Diphosphate-N-Acetylglucosamine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000068701 | 1 – 456 | Bifunctional protein GlmUAdd BLAST | 456 |
Proteomic databases
jPOSTi | P0ACC7 |
PaxDbi | P0ACC7 |
PRIDEi | P0ACC7 |
Interactioni
Subunit structurei
Homotrimer. In vivo forms a hexameric aggregate.
5 PublicationsBinary interactionsi
P0ACC7
With | #Exp. | IntAct |
---|---|---|
rpsB [P0A7V0] | 2 | EBI-370256,EBI-543439 |
GO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4262143, 312 interactors 852548, 1 interactor |
DIPi | DIP-31844N |
IntActi | P0ACC7, 19 interactors |
STRINGi | 511145.b3730 |
Chemistry databases
BindingDBi | P0ACC7 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0ACC7 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0ACC7 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 229 | PyrophosphorylaseUniRule annotation2 PublicationsAdd BLAST | 229 | |
Regioni | 11 – 14 | UDP-GlcNAc bindingUniRule annotation3 Publications | 4 | |
Regioni | 81 – 82 | UDP-GlcNAc bindingUniRule annotation3 Publications | 2 | |
Regioni | 103 – 105 | UDP-GlcNAc bindingUniRule annotation3 Publications | 3 | |
Regioni | 230 – 250 | LinkerUniRule annotation2 PublicationsAdd BLAST | 21 | |
Regioni | 251 – 456 | N-acetyltransferaseUniRule annotation2 PublicationsAdd BLAST | 206 | |
Regioni | 386 – 387 | Acetyl-CoA bindingUniRule annotation | 2 |
Sequence similaritiesi
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.UniRule annotationCurated
In the C-terminal section; belongs to the transferase hexapeptide repeat family.UniRule annotationCurated
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | COG1207, Bacteria |
HOGENOMi | CLU_029499_15_2_6 |
InParanoidi | P0ACC7 |
PhylomeDBi | P0ACC7 |
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 IPR018357, Hexapep_transf_CS IPR025877, MobA-like_NTP_Trfase IPR029044, Nucleotide-diphossugar_trans IPR011004, Trimer_LpxA-like_sf |
Pfami | View protein in Pfam PF00132, Hexapep, 2 hits PF14602, Hexapep_2, 1 hit PF12804, NTP_transf_3, 1 hit |
SUPFAMi | SSF51161, SSF51161, 1 hit SSF53448, SSF53448, 1 hit |
TIGRFAMsi | TIGR01173, glmU, 1 hit |
PROSITEi | View protein in PROSITE PS00101, HEXAPEP_TRANSFERASES, 1 hit |
i Sequence
Sequence statusi: Complete.
P0ACC7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH
60 70 80 90 100
VHLVYGHGGD LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL
110 120 130 140 150
MLYGDVPLIS VETLQRLRDA KPQGGIGLLT VKLDDPTGYG RITRENGKVT
160 170 180 190 200
GIVEHKDATD EQRQIQEINT GILIANGADM KRWLAKLTNN NAQGEYYITD
210 220 230 240 250
IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ SEQAEKLLLA
260 270 280 290 300
GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN
310 320 330 340 350
SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM
360 370 380 390 400
KKARLGKGSK AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD
410 420 430 440 450
VFVGSDTQLV APVTVGKGAT IAAGTTVTRN VGENALAISR VPQTQKEGWR
RPVKKK
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 186 – 187 | KL → NV in CAA25784 (PubMed:6395859).Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X01631 Genomic DNA Translation: CAA25784.1 L10328 Genomic DNA Translation: AAA62082.1 Frameshift. L10328 Genomic DNA Translation: AAA62081.1 Frameshift. U00096 Genomic DNA Translation: AAC76753.1 AP009048 Genomic DNA Translation: BAE77558.1 |
PIRi | C65176 |
RefSeqi | NP_418186.1, NC_000913.3 WP_000933736.1, NZ_STEB01000015.1 |
Genome annotation databases
EnsemblBacteriai | AAC76753; AAC76753; b3730 BAE77558; BAE77558; BAE77558 |
GeneIDi | 66672366 948246 |
KEGGi | ecj:JW3708 eco:b3730 |
PATRICi | fig|1411691.4.peg.2970 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X01631 Genomic DNA Translation: CAA25784.1 L10328 Genomic DNA Translation: AAA62082.1 Frameshift. L10328 Genomic DNA Translation: AAA62081.1 Frameshift. U00096 Genomic DNA Translation: AAC76753.1 AP009048 Genomic DNA Translation: BAE77558.1 |
PIRi | C65176 |
RefSeqi | NP_418186.1, NC_000913.3 WP_000933736.1, NZ_STEB01000015.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1FWY | X-ray | 2.30 | A/B | 1-331 | [»] | |
1FXJ | X-ray | 2.25 | A/B | 1-331 | [»] | |
1HV9 | X-ray | 2.10 | A/B | 1-456 | [»] | |
2OI5 | X-ray | 2.25 | A/B | 1-456 | [»] | |
2OI6 | X-ray | 2.20 | A/B | 1-456 | [»] | |
2OI7 | X-ray | 2.54 | A/B | 1-456 | [»] | |
3TWD | X-ray | 1.90 | A/B | 233-452 | [»] | |
4AA7 | X-ray | 2.00 | A/B | 227-456 | [»] | |
SMRi | P0ACC7 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262143, 312 interactors 852548, 1 interactor |
DIPi | DIP-31844N |
IntActi | P0ACC7, 19 interactors |
STRINGi | 511145.b3730 |
Chemistry databases
BindingDBi | P0ACC7 |
ChEMBLi | CHEMBL3414415 |
DrugBanki | DB03814, 2-(N-morpholino)ethanesulfonic acid DB01992, Coenzyme A DB03397, Uridine-Diphosphate-N-Acetylglucosamine |
Proteomic databases
jPOSTi | P0ACC7 |
PaxDbi | P0ACC7 |
PRIDEi | P0ACC7 |
Genome annotation databases
EnsemblBacteriai | AAC76753; AAC76753; b3730 BAE77558; BAE77558; BAE77558 |
GeneIDi | 66672366 948246 |
KEGGi | ecj:JW3708 eco:b3730 |
PATRICi | fig|1411691.4.peg.2970 |
Organism-specific databases
EchoBASEi | EB1184 |
Phylogenomic databases
eggNOGi | COG1207, Bacteria |
HOGENOMi | CLU_029499_15_2_6 |
InParanoidi | P0ACC7 |
PhylomeDBi | P0ACC7 |
Enzyme and pathway databases
UniPathwayi | UPA00113;UER00532 UPA00113;UER00533 UPA00973 |
BioCyci | EcoCyc:NAG1P-URIDYLTRANS-MONOMER |
BRENDAi | 2.3.1.157, 2026 2.7.7.23, 2026 |
SABIO-RKi | P0ACC7 |
Miscellaneous databases
EvolutionaryTracei | P0ACC7 |
PROi | PR:P0ACC7 |
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 IPR018357, Hexapep_transf_CS IPR025877, MobA-like_NTP_Trfase IPR029044, Nucleotide-diphossugar_trans IPR011004, Trimer_LpxA-like_sf |
Pfami | View protein in Pfam PF00132, Hexapep, 2 hits PF14602, Hexapep_2, 1 hit PF12804, NTP_transf_3, 1 hit |
SUPFAMi | SSF51161, SSF51161, 1 hit SSF53448, SSF53448, 1 hit |
TIGRFAMsi | TIGR01173, glmU, 1 hit |
PROSITEi | View protein in PROSITE PS00101, HEXAPEP_TRANSFERASES, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | GLMU_ECOLI | |
Accessioni | P0ACC7Primary (citable) accession number: P0ACC7 Secondary accession number(s): P17114, P76746, Q2M848 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 8, 2005 |
Last sequence update: | November 8, 2005 | |
Last modified: | February 23, 2022 | |
This is version 138 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