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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 Publications

Catalytic activityi

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation3 Publications
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.UniRule 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

Enzyme 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

  1. KM=0.018 mM for N-acetylglucosamine 1-phosphate3 Publications
  2. KM=0.07 mM for alpha-D-glucosamine 1-phosphate1 Publication
  3. KM=0.1 mM for UTP1 Publication
  4. KM=0.15 mM for alpha-D-glucosamine 1-phosphate3 Publications
  5. KM=0.25 mM for alpha-D-glucosamine 1-phosphate3 Publications
  6. KM=0.32 mM for acetyl-CoA3 Publications
  7. KM=0.6 mM for acetyl-CoA3 Publications
  8. KM=0.84 mM for n-propionyl-CoA3 Publications
  9. KM=1.3 mM for UDP-glucosamine3 Publications
  10. KM=2 mM for glucose-1-P3 Publications
  11. KM=3.7 mM for N-acetylgalactosamine-1-P3 Publications
  12. KM=15 mM for galactosamine-1-phosphate3 Publications

    Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

    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
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Bifunctional protein GlmU (glmU)
    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
    Proteins known to be involved in this subpathway in this organism are:
    1. Bifunctional protein GlmU (glmU)
    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 annotation
    View 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 keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei25UDP-GlcNAcUniRule annotation1
    Binding sitei76UDP-GlcNAcUniRule annotation3 Publications1
    Metal bindingi105Magnesium or cobalt2 Publications1
    Binding sitei140UDP-GlcNAc; via amide nitrogenUniRule annotation3 Publications1
    Binding sitei154UDP-GlcNAcUniRule annotation3 Publications1
    Binding sitei169UDP-GlcNAcUniRule annotation3 Publications1
    Metal bindingi227Magnesium or cobalt2 Publications1
    Binding sitei227UDP-GlcNAcUniRule annotation1
    Binding sitei333UDP-GlcNAcUniRule annotation2 Publications1
    Binding sitei351UDP-GlcNAcUniRule annotation2 Publications1
    Active sitei363Proton acceptorUniRule annotation1
    Binding sitei366UDP-GlcNAcUniRule annotation2 Publications1
    Binding sitei377UDP-GlcNAcUniRule annotation3 Publications1
    Binding sitei380Acetyl-CoA; via amide nitrogenUniRule annotation2 Publications1
    Binding sitei405Acetyl-CoAUniRule annotation3 Publications1
    Binding sitei423Acetyl-CoA; via amide nitrogenUniRule annotation3 Publications1
    Binding sitei440Acetyl-CoAUniRule annotation3 Publications1

    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

    Keywordsi

    Molecular functionAcyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Transferase
    Biological processCell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
    LigandCobalt, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:NAG1P-URIDYLTRANS-MONOMER
    MetaCyc:NAG1P-URIDYLTRANS-MONOMER
    BRENDAi2.3.1.157 2026
    2.7.7.23 2026
    SABIO-RKiP0ACC7
    UniPathwayiUPA00113; UER00532
    UPA00113; UER00533
    UPA00973

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional protein GlmUUniRule annotation
    Including 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
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11198 glmU

    Subcellular locationi

    • Cytoplasm UniRule annotation1 Publication

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi14G → A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP. 1 Publication1
    Mutagenesisi18R → A: Dramatically impairs the uridyltransferase activity. 1 Publication1
    Mutagenesisi25K → A: 8-fold decrease in uridyltransferase activity. 1 Publication1
    Mutagenesisi296C → A: No effect. 1 Publication1
    Mutagenesisi307C → A: 1350-fold decrease in acetyltransferase activity. 1 Publication1
    Mutagenesisi324C → A: 8-fold decrease in acetyltransferase activity. 1 Publication1
    Mutagenesisi385C → A: No effect. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL3414415
    DrugBankiDB03814 2-(N-Morpholino)-Ethanesulfonic Acid
    DB01992 Coenzyme A
    DB03397 Uridine-Diphosphate-N-Acetylglucosamine

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000687011 – 456Bifunctional protein GlmUAdd BLAST456

    Proteomic databases

    PaxDbiP0ACC7
    PRIDEiP0ACC7

    Interactioni

    Subunit structurei

    Homotrimer. In vivo forms a hexameric aggregate.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rpsBP0A7V02EBI-370256,EBI-543439

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4262143, 312 interactors
    DIPiDIP-31844N
    IntActiP0ACC7, 19 interactors
    STRINGi316385.ECDH10B_3917

    Chemistry databases

    BindingDBiP0ACC7

    Structurei

    Secondary structure

    1456
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 12Combined sources7
    Helixi17 – 19Combined sources3
    Helixi25 – 27Combined sources3
    Beta strandi28 – 30Combined sources3
    Helixi35 – 46Combined sources12
    Beta strandi51 – 55Combined sources5
    Helixi59 – 65Combined sources7
    Turni66 – 68Combined sources3
    Beta strandi71 – 75Combined sources5
    Helixi82 – 89Combined sources8
    Helixi90 – 92Combined sources3
    Beta strandi97 – 103Combined sources7
    Helixi111 – 120Combined sources10
    Beta strandi125 – 132Combined sources8
    Beta strandi141 – 145Combined sources5
    Beta strandi148 – 153Combined sources6
    Turni155 – 157Combined sources3
    Helixi162 – 164Combined sources3
    Beta strandi167 – 176Combined sources10
    Helixi177 – 184Combined sources8
    Beta strandi191 – 193Combined sources3
    Helixi198 – 200Combined sources3
    Helixi201 – 206Combined sources6
    Turni207 – 209Combined sources3
    Beta strandi212 – 215Combined sources4
    Helixi220 – 223Combined sources4
    Helixi233 – 249Combined sources17
    Beta strandi253 – 255Combined sources3
    Helixi257 – 259Combined sources3
    Beta strandi260 – 268Combined sources9
    Beta strandi278 – 286Combined sources9
    Beta strandi297 – 300Combined sources4
    Beta strandi314 – 317Combined sources4
    Beta strandi325 – 327Combined sources3
    Beta strandi328 – 332Combined sources5
    Beta strandi336 – 338Combined sources3
    Beta strandi343 – 355Combined sources13
    Beta strandi360 – 372Combined sources13
    Beta strandi383 – 385Combined sources3
    Beta strandi387 – 390Combined sources4
    Beta strandi395 – 397Combined sources3
    Beta strandi408 – 415Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FWYX-ray2.30A/B1-331[»]
    1FXJX-ray2.25A/B1-331[»]
    1HV9X-ray2.10A/B1-456[»]
    2OI5X-ray2.25A/B1-456[»]
    2OI6X-ray2.20A/B1-456[»]
    2OI7X-ray2.54A/B1-456[»]
    3TWDX-ray1.90A/B233-452[»]
    4AA7X-ray2.00A/B227-456[»]
    ProteinModelPortaliP0ACC7
    SMRiP0ACC7
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ACC7

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 229PyrophosphorylaseUniRule annotation2 PublicationsAdd BLAST229
    Regioni11 – 14UDP-GlcNAc bindingUniRule annotation3 Publications4
    Regioni81 – 82UDP-GlcNAc bindingUniRule annotation3 Publications2
    Regioni103 – 105UDP-GlcNAc bindingUniRule annotation3 Publications3
    Regioni230 – 250LinkerUniRule annotation2 PublicationsAdd BLAST21
    Regioni251 – 456N-acetyltransferaseUniRule annotation2 PublicationsAdd BLAST206
    Regioni386 – 387Acetyl-CoA bindingUniRule annotation2

    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

    Repeat

    Phylogenomic databases

    eggNOGiENOG4105CAJ Bacteria
    COG1207 LUCA
    HOGENOMiHOG000283476
    InParanoidiP0ACC7
    KOiK04042
    OMAiIEPQTHL
    PhylomeDBiP0ACC7

    Family and domain databases

    CDDicd03353 LbH_GlmU_C, 1 hit
    Gene3Di3.90.550.10, 1 hit
    HAMAPiMF_01631 GlmU, 1 hit
    InterProiView 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
    PfamiView protein in Pfam
    PF00132 Hexapep, 3 hits
    PF12804 NTP_transf_3, 1 hit
    SUPFAMiSSF51161 SSF51161, 1 hit
    SSF53448 SSF53448, 1 hit
    TIGRFAMsiTIGR01173 glmU, 1 hit
    PROSITEiView protein in PROSITE
    PS00101 HEXAPEP_TRANSFERASES, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P0ACC7-1 [UniParc]FASTAAdd to basket

    « Hide

            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
    Length:456
    Mass (Da):49,190
    Last modified:November 8, 2005 - v1
    Checksum:i2F3C5C84F673C8A3
    GO

    Sequence cautioni

    The sequence AAA62081 differs from that shown. Reason: Frameshift at position 179. Produces two ORFs.Curated
    The sequence AAA62082 differs from that shown. Reason: Frameshift at position 179. Produces two ORFs.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti186 – 187KL → NV in CAA25784 (PubMed:6395859).Curated2

    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
    PIRiC65176
    RefSeqiNP_418186.1, NC_000913.3
    WP_000933736.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC76753; AAC76753; b3730
    BAE77558; BAE77558; BAE77558
    GeneIDi948246
    KEGGiecj:JW3708
    eco:b3730
    PATRICifig|1411691.4.peg.2970

    Similar proteinsi

    Entry informationi

    Entry nameiGLMU_ECOLI
    AccessioniPrimary (citable) accession number: P0ACC7
    Secondary accession number(s): P17114, P76746, Q2M848
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: March 28, 2018
    This is version 115 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health