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Q04DS4

- GLMU_OENOB

UniProt

Q04DS4 - GLMU_OENOB

Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Oenococcus oeni (strain ATCC BAA-331 / PSU-1)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (14 Nov 2006)
      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.UniRule annotation

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium ion per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei23 – 231UDP-GlcNAcUniRule annotation
    Binding sitei69 – 691UDP-GlcNAcUniRule annotation
    Metal bindingi97 – 971MagnesiumUniRule annotation
    Binding sitei132 – 1321UDP-GlcNAc; via amide nitrogenUniRule annotation
    Binding sitei148 – 1481UDP-GlcNAcUniRule annotation
    Binding sitei163 – 1631UDP-GlcNAcUniRule annotation
    Metal bindingi214 – 2141MagnesiumUniRule annotation
    Binding sitei214 – 2141UDP-GlcNAcUniRule annotation
    Binding sitei286 – 2861Acetyl-CoA; amide nitrogenUniRule annotation
    Binding sitei304 – 3041Acetyl-CoAUniRule annotation
    Active sitei316 – 3161Proton acceptorUniRule annotation
    Binding sitei319 – 3191Acetyl-CoAUniRule annotation
    Binding sitei330 – 3301Acetyl-CoAUniRule annotation
    Binding sitei358 – 3581Acetyl-CoAUniRule annotation
    Binding sitei376 – 3761Acetyl-CoA; via amide nitrogenUniRule annotation
    Binding sitei393 – 3931Acetyl-CoAUniRule annotation

    GO - Molecular functioni

    1. glucosamine-1-phosphate N-acetyltransferase activity Source: UniProtKB-HAMAP
    2. magnesium ion binding Source: UniProtKB-HAMAP
    3. UDP-N-acetylglucosamine diphosphorylase activity Source: UniProtKB-HAMAP

    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: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Acyltransferase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciOOEN203123:GHNL-1542-MONOMER.
    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 annotation)
    Alternative name(s):
    N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation
    Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation)
    Gene namesi
    Name:glmUUniRule annotation
    Ordered Locus Names:OEOE_1542
    OrganismiOenococcus oeni (strain ATCC BAA-331 / PSU-1)
    Taxonomic identifieri203123 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeOenococcus
    ProteomesiUP000000774: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 426426Bifunctional protein GlmUPRO_1000069734Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi203123.OEOE_1542.

    Structurei

    3D structure databases

    ProteinModelPortaliQ04DS4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 216216PyrophosphorylaseUniRule annotationAdd
    BLAST
    Regioni9 – 124UDP-GlcNAc bindingUniRule annotation
    Regioni217 – 23721LinkerUniRule annotationAdd
    BLAST
    Regioni238 – 426189N-acetyltransferaseUniRule annotationAdd
    BLAST
    Regioni339 – 3402Acetyl-CoA bindingUniRule annotation

    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

    Repeat

    Phylogenomic databases

    eggNOGiCOG1207.
    HOGENOMiHOG000283476.
    KOiK04042.
    OMAiCNIAAGT.
    OrthoDBiEOG6Z6FQZ.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    HAMAPiMF_01631. GlmU.
    InterProiIPR005882. Bifunctional_GlmU.
    IPR001451. Hexapep_transf.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q04DS4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEVDVVILA AGKGSRMKDD LSKPLHKVAG LPMLEWICRA VRKFNPKNII    50
    AVQGADEDFS SYVDETVVQK EQLGSADALR CAFPKIDAEK LIVINADMPL 100
    MTENDLVDLV EKGEGFDAAL LTADLKKPFG YGRVIPVGER NVVEQIVEER 150
    DATADQKKLH LVNAGVYLFR ADYIKRAINN VTTDNSQSEY YLTDALPGAK 200
    IVQVADWHDI LGVNTQQQLA AVSKIARKRI NDQIMANGVT MIDPLTTYID 250
    ANVLVGTGTI IKPGTVIEHD SVIGAENEIG PYAHLREKTV TGIDVHIGNF 300
    VETKNAKIGD HTHIGHLTYV GDAEVGQAVN IGAGTIFVNY DGKNKHMTKV 350
    GDRAFIGSNS KLVAPVEIAS EAITAAGSTI TDNVDQHAMG IARQRQTNKS 400
    DFWQRMPHED FATEYDAKHD QRDDQP 426
    Length:426
    Mass (Da):46,641
    Last modified:November 14, 2006 - v1
    Checksum:iCCDF7323AEBC1E01
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000411 Genomic DNA. Translation: ABJ57398.1.
    RefSeqiWP_011677759.1. NC_008528.1.
    YP_811063.1. NC_008528.1.

    Genome annotation databases

    EnsemblBacteriaiABJ57398; ABJ57398; OEOE_1542.
    GeneIDi4415811.
    KEGGiooe:OEOE_1542.
    PATRICi22801324. VBIOenOen113004_1568.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000411 Genomic DNA. Translation: ABJ57398.1 .
    RefSeqi WP_011677759.1. NC_008528.1.
    YP_811063.1. NC_008528.1.

    3D structure databases

    ProteinModelPortali Q04DS4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 203123.OEOE_1542.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABJ57398 ; ABJ57398 ; OEOE_1542 .
    GeneIDi 4415811.
    KEGGi ooe:OEOE_1542.
    PATRICi 22801324. VBIOenOen113004_1568.

    Phylogenomic databases

    eggNOGi COG1207.
    HOGENOMi HOG000283476.
    KOi K04042.
    OMAi CNIAAGT.
    OrthoDBi EOG6Z6FQZ.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00532 .
    UPA00113 ; UER00533 .
    UPA00973 .
    BioCyci OOEN203123:GHNL-1542-MONOMER.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    HAMAPi MF_01631. GlmU.
    InterProi IPR005882. Bifunctional_GlmU.
    IPR001451. Hexapep_transf.
    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-331 / PSU-1.

    Entry informationi

    Entry nameiGLMU_OENOB
    AccessioniPrimary (citable) accession number: Q04DS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: November 14, 2006
    Last modified: October 1, 2014
    This is version 66 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

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3