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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.2 Publications

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Co2+1 PublicationNote: Binds 1 Mg(2+) ion per subunit. Can also use Co2+ ion to a lesser extent.1 Publication

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

    Pathway:iUDP-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).
    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.

    Pathway:iUDP-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.
    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.

    Pathway:iLPS lipid A biosynthesis

    This protein is involved in the pathway LPS lipid A biosynthesis, which is part of Bacterial outer membrane biogenesis.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei25 – 251UDP-GlcNAcBy similarity
    Binding sitei76 – 761UDP-GlcNAc3 Publications
    Metal bindingi105 – 1051Magnesium
    Binding sitei140 – 1401UDP-GlcNAc; via amide nitrogen3 Publications
    Binding sitei154 – 1541UDP-GlcNAc3 Publications
    Binding sitei169 – 1691UDP-GlcNAc3 Publications
    Metal bindingi227 – 2271Magnesium
    Binding sitei227 – 2271UDP-GlcNAcBy similarity
    Binding sitei333 – 3331UDP-GlcNAc3 Publications
    Binding sitei351 – 3511UDP-GlcNAc3 Publications
    Active sitei363 – 3631Proton acceptorBy similarity
    Binding sitei366 – 3661UDP-GlcNAc3 Publications
    Binding sitei377 – 3771UDP-GlcNAc3 Publications
    Binding sitei380 – 3801Acetyl-CoA; via amide nitrogen
    Binding sitei405 – 4051Acetyl-CoA
    Binding sitei423 – 4231Acetyl-CoA; via amide nitrogen
    Binding sitei440 – 4401Acetyl-CoA

    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

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Keywords - Ligandi

    Cobalt, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:NAG1P-URIDYLTRANS-MONOMER.
    ECOL316407:JW3708-MONOMER.
    MetaCyc:NAG1P-URIDYLTRANS-MONOMER.
    BRENDAi2.3.1.157. 2026.
    2.7.7.23. 2026.
    SABIO-RKP0ACC7.
    UniPathwayiUPA00113; UER00532.
    UPA00113; UER00533.
    UPA00973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional protein GlmU
    Including the following 2 domains:
    UDP-N-acetylglucosamine pyrophosphorylase (EC:2.7.7.23)
    Alternative name(s):
    N-acetylglucosamine-1-phosphate uridyltransferase
    Glucosamine-1-phosphate N-acetyltransferase (EC:2.3.1.157)
    Gene namesi
    Name:glmU
    Synonyms:yieA
    Ordered Locus Names:b3730, JW3708
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11198. glmU.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141G → A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP. 1 Publication
    Mutagenesisi18 – 181R → A: Dramatically impairs the uridyltransferase activity. 1 Publication
    Mutagenesisi25 – 251K → A: 8-fold decrease in uridyltransferase activity. 1 Publication
    Mutagenesisi296 – 2961C → A: No effect. 1 Publication
    Mutagenesisi307 – 3071C → A: 1350-fold decrease in acetyltransferase activity. 1 Publication
    Mutagenesisi324 – 3241C → A: 8-fold decrease in acetyltransferase activity. 1 Publication
    Mutagenesisi385 – 3851C → A: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 456456Bifunctional protein GlmUPRO_0000068701Add
    BLAST

    Proteomic databases

    PaxDbiP0ACC7.
    PRIDEiP0ACC7.

    Interactioni

    Subunit structurei

    Homotrimer. In vivo forms a hexameric aggregate.5 Publications

    Protein-protein interaction databases

    DIPiDIP-31844N.
    IntActiP0ACC7. 19 interactions.
    MINTiMINT-1252604.
    STRINGi511145.b3730.

    Structurei

    Secondary structure

    1
    456
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127Combined sources
    Helixi17 – 193Combined sources
    Helixi25 – 273Combined sources
    Beta strandi28 – 303Combined sources
    Helixi35 – 4612Combined sources
    Beta strandi51 – 555Combined sources
    Helixi59 – 657Combined sources
    Turni66 – 683Combined sources
    Beta strandi71 – 755Combined sources
    Helixi82 – 898Combined sources
    Helixi90 – 923Combined sources
    Beta strandi97 – 1037Combined sources
    Helixi111 – 12010Combined sources
    Beta strandi125 – 1328Combined sources
    Beta strandi141 – 1455Combined sources
    Beta strandi148 – 1536Combined sources
    Turni155 – 1573Combined sources
    Helixi162 – 1643Combined sources
    Beta strandi167 – 17610Combined sources
    Helixi177 – 1848Combined sources
    Beta strandi191 – 1933Combined sources
    Helixi198 – 2003Combined sources
    Helixi201 – 2066Combined sources
    Turni207 – 2093Combined sources
    Beta strandi212 – 2154Combined sources
    Helixi220 – 2234Combined sources
    Helixi233 – 24917Combined sources
    Beta strandi253 – 2553Combined sources
    Helixi257 – 2593Combined sources
    Beta strandi260 – 2689Combined sources
    Beta strandi278 – 2869Combined sources
    Beta strandi297 – 3004Combined sources
    Beta strandi314 – 3174Combined sources
    Beta strandi325 – 3273Combined sources
    Beta strandi328 – 3325Combined sources
    Beta strandi336 – 3383Combined sources
    Beta strandi343 – 35513Combined sources
    Beta strandi360 – 37213Combined sources
    Beta strandi383 – 3853Combined sources
    Beta strandi387 – 3904Combined sources
    Beta strandi395 – 3973Combined sources
    Beta strandi408 – 4158Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 3-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ACC7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 229229PyrophosphorylaseAdd
    BLAST
    Regioni11 – 144UDP-GlcNAc binding
    Regioni81 – 822UDP-GlcNAc binding
    Regioni103 – 1053UDP-GlcNAc binding
    Regioni230 – 25021LinkerAdd
    BLAST
    Regioni251 – 456206N-acetyltransferaseAdd
    BLAST
    Regioni386 – 3872Acetyl-CoA binding

    Sequence similaritiesi

    In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.Curated
    In the C-terminal section; belongs to the transferase hexapeptide repeat family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1207.
    HOGENOMiHOG000283476.
    InParanoidiP0ACC7.
    KOiK04042.
    OMAiFAHARPK.
    OrthoDBiEOG6Z6FQZ.
    PhylomeDBiP0ACC7.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    HAMAPiMF_01631. GlmU.
    InterProiIPR005882. Bifunctional_GlmU.
    IPR001451. Hexapep_transf.
    IPR018357. Hexapep_transf_CS.
    IPR025877. MobA-like_NTP_Trfase_dom.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR011004. Trimer_LpxA-like.
    [Graphical view]
    PfamiPF00132. Hexapep. 3 hits.
    PF12804. NTP_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF51161. SSF51161. 1 hit.
    SSF53448. SSF53448. 1 hit.
    TIGRFAMsiTIGR01173. glmU. 1 hit.
    PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
    [Graphical view]

    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 AAA62081.1 differs from that shown. Reason: Frameshift at position 179. Produces two ORFs.Curated
    The sequence AAA62082.1 differs from that shown. Reason: Frameshift at position 179. Produces two ORFs.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1872KL → NV in CAA25784 (PubMed:6395859).Curated

    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_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76753; AAC76753; b3730.
    BAE77558; BAE77558; BAE77558.
    GeneIDi948246.
    KEGGieco:b3730.
    PATRICi32122957. VBIEscCol129921_3854.

    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.
    PIRiC65176.
    RefSeqiNP_418186.1. NC_000913.3.
    WP_000933736.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 3-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-31844N.
    IntActiP0ACC7. 19 interactions.
    MINTiMINT-1252604.
    STRINGi511145.b3730.

    Chemistry

    BindingDBiP0ACC7.

    Proteomic databases

    PaxDbiP0ACC7.
    PRIDEiP0ACC7.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76753; AAC76753; b3730.
    BAE77558; BAE77558; BAE77558.
    GeneIDi948246.
    KEGGieco:b3730.
    PATRICi32122957. VBIEscCol129921_3854.

    Organism-specific databases

    EchoBASEiEB1184.
    EcoGeneiEG11198. glmU.

    Phylogenomic databases

    eggNOGiCOG1207.
    HOGENOMiHOG000283476.
    InParanoidiP0ACC7.
    KOiK04042.
    OMAiFAHARPK.
    OrthoDBiEOG6Z6FQZ.
    PhylomeDBiP0ACC7.

    Enzyme and pathway databases

    UniPathwayiUPA00113; UER00532.
    UPA00113; UER00533.
    UPA00973.
    BioCyciEcoCyc:NAG1P-URIDYLTRANS-MONOMER.
    ECOL316407:JW3708-MONOMER.
    MetaCyc:NAG1P-URIDYLTRANS-MONOMER.
    BRENDAi2.3.1.157. 2026.
    2.7.7.23. 2026.
    SABIO-RKP0ACC7.

    Miscellaneous databases

    EvolutionaryTraceiP0ACC7.
    PROiP0ACC7.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    HAMAPiMF_01631. GlmU.
    InterProiIPR005882. Bifunctional_GlmU.
    IPR001451. Hexapep_transf.
    IPR018357. Hexapep_transf_CS.
    IPR025877. MobA-like_NTP_Trfase_dom.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR011004. Trimer_LpxA-like.
    [Graphical view]
    PfamiPF00132. Hexapep. 3 hits.
    PF12804. NTP_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF51161. SSF51161. 1 hit.
    SSF53448. SSF53448. 1 hit.
    TIGRFAMsiTIGR01173. glmU. 1 hit.
    PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS."
      Walker J.E., Gay N.J., Saraste M., Eberle A.N.
      Biochem. J. 224:799-815(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
      Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
      Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli."
      Mengin-Lecreulx D., van Heijenoort J.
      J. Bacteriol. 175:6150-6157(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    6. "Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis."
      Mengin-Lecreulx D., van Heijenoort J.
      J. Bacteriol. 176:5788-5795(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    7. "Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."
      Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.
      Biochemistry 35:579-585(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional protein glmU from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes."
      Pompeo F., van Heijenoort J., Mengin-Lecreulx D.
      J. Bacteriol. 180:4799-4803(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily."
      Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.
      EMBO J. 18:4096-4107(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX WITH UDP-GLCNAC, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25.
    10. "Structure of the Escherichia coli glmU pyrophosphorylase and acetyltransferase active sites."
      Olsen L.R., Roderick S.L.
      Biochemistry 40:1913-1921(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC AND COA, COFACTOR, SUBUNIT.
    11. "Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products."
      Olsen L.R., Vetting M.W., Roderick S.L.
      Protein Sci. 16:1230-1235(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC, COA AND MAGNESIUM IONS, SUBUNIT.
    12. "In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae."
      Buurman E.T., Andrews B., Gao N., Hu J., Keating T.A., Lahiri S., Otterbein L.R., Patten A.D., Stokes S.S., Shapiro A.B.
      J. Biol. Chem. 286:40734-40742(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 233-452, ENZYME REGULATION, SUBUNIT.
    13. "Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 1: Hit to lead evaluation of a novel arylsulfonamide series."
      Green O.M., McKenzie A.R., Shapiro A.B., Otterbein L., Ni H., Patten A., Stokes S., Albert R., Kawatkar S., Breed J.
      Bioorg. Med. Chem. Lett. 22:1510-1519(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 227-456, ENZYME REGULATION, SUBUNIT.

    Entry informationi

    Entry nameiGLMU_ECOLI
    AccessioniPrimary (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: July 22, 2015
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.