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P0ACC7

- GLMU_ECOLI

UniProt

P0ACC7 - GLMU_ECOLI

Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (08 Nov 2005)
      Previous versions | rss
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    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

    Binds 1 magnesium ion per subunit. Can also use cobalt ions 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

    Pathwayi

    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

    1. glucosamine-1-phosphate N-acetyltransferase activity Source: EcoCyc
    2. identical protein binding Source: EcoCyc
    3. magnesium ion binding Source: EcoCyc
    4. UDP-N-acetylglucosamine diphosphorylase activity Source: EcoCyc

    GO - Biological processi

    1. cell morphogenesis Source: UniProtKB-HAMAP
    2. lipid A biosynthetic process Source: UniProtKB-UniPathway
    3. lipopolysaccharide biosynthetic process Source: InterPro
    4. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
    5. regulation of cell shape Source: UniProtKB-KW
    6. UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11198. glmU.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ACC7.

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK04042.
    OMAiDCVTNQD.
    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

    MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH    50
    VHLVYGHGGD LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL 100
    MLYGDVPLIS VETLQRLRDA KPQGGIGLLT VKLDDPTGYG RITRENGKVT 150
    GIVEHKDATD EQRQIQEINT GILIANGADM KRWLAKLTNN NAQGEYYITD 200
    IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ SEQAEKLLLA 250
    GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN 300
    SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM 350
    KKARLGKGSK AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD 400
    VFVGSDTQLV APVTVGKGAT IAAGTTVTRN VGENALAISR VPQTQKEGWR 450
    RPVKKK 456
    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.
    The sequence AAA62082.1 differs from that shown. Reason: Frameshift at position 179. Produces two ORFs.

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491699.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76753; AAC76753; b3730.
    BAE77558; BAE77558; BAE77558.
    GeneIDi12933149.
    948246.
    KEGGiecj:Y75_p3438.
    eco:b3730.
    PATRICi32122957. VBIEscCol129921_3854.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491699.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P0ACC7.
    SMRi P0ACC7. Positions 3-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31844N.
    IntActi P0ACC7. 19 interactions.
    MINTi MINT-1252604.
    STRINGi 511145.b3730.

    Proteomic databases

    PaxDbi P0ACC7.
    PRIDEi P0ACC7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76753 ; AAC76753 ; b3730 .
    BAE77558 ; BAE77558 ; BAE77558 .
    GeneIDi 12933149.
    948246.
    KEGGi ecj:Y75_p3438.
    eco:b3730.
    PATRICi 32122957. VBIEscCol129921_3854.

    Organism-specific databases

    EchoBASEi EB1184.
    EcoGenei EG11198. glmU.

    Phylogenomic databases

    eggNOGi COG1207.
    HOGENOMi HOG000283476.
    KOi K04042.
    OMAi DCVTNQD.
    OrthoDBi EOG6Z6FQZ.
    PhylomeDBi P0ACC7.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00532 .
    UPA00113 ; UER00533 .
    UPA00973 .
    BioCyci EcoCyc:NAG1P-URIDYLTRANS-MONOMER.
    ECOL316407:JW3708-MONOMER.
    MetaCyc:NAG1P-URIDYLTRANS-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ACC7.
    PROi P0ACC7.

    Gene expression databases

    Genevestigatori P0ACC7.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    HAMAPi MF_01631. GlmU.
    InterProi IPR005882. 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 ]
    Pfami PF00132. Hexapep. 3 hits.
    PF12804. NTP_transf_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51161. SSF51161. 1 hit.
    SSF53448. SSF53448. 1 hit.
    TIGRFAMsi TIGR01173. glmU. 1 hit.
    PROSITEi PS00101. HEXAPEP_TRANSFERASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 90 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