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A2RMV7

- GLMU_LACLM

UniProt

A2RMV7 - GLMU_LACLM

Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      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 sitei22 – 221UDP-GlcNAcUniRule annotation
    Binding sitei72 – 721UDP-GlcNAcUniRule annotation
    Metal bindingi102 – 1021MagnesiumUniRule annotation
    Binding sitei139 – 1391UDP-GlcNAc; via amide nitrogenUniRule annotation
    Binding sitei154 – 1541UDP-GlcNAcUniRule annotation
    Binding sitei169 – 1691UDP-GlcNAcUniRule annotation
    Metal bindingi227 – 2271MagnesiumUniRule annotation
    Binding sitei227 – 2271UDP-GlcNAcUniRule annotation
    Binding sitei332 – 3321Acetyl-CoA; amide nitrogenUniRule annotation
    Binding sitei350 – 3501Acetyl-CoAUniRule annotation
    Active sitei362 – 3621Proton acceptorUniRule annotation
    Binding sitei365 – 3651Acetyl-CoAUniRule annotation
    Binding sitei376 – 3761Acetyl-CoAUniRule annotation
    Binding sitei404 – 4041Acetyl-CoAUniRule annotation
    Binding sitei422 – 4221Acetyl-CoA; via amide nitrogenUniRule annotation
    Binding sitei439 – 4391Acetyl-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

    BioCyciLLAC416870:GCDT-2078-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:llmg_2076
    OrganismiLactococcus lactis subsp. cremoris (strain MG1363)
    Taxonomic identifieri416870 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
    ProteomesiUP000000364: 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 – 458458Bifunctional protein GlmUPRO_1000056169Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi416870.llmg_2076.

    Structurei

    3D structure databases

    ProteinModelPortaliA2RMV7.
    SMRiA2RMV7. Positions 2-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 229229PyrophosphorylaseUniRule annotationAdd
    BLAST
    Regioni8 – 114UDP-GlcNAc bindingUniRule annotation
    Regioni77 – 782UDP-GlcNAc bindingUniRule annotation
    Regioni230 – 25021LinkerUniRule annotationAdd
    BLAST
    Regioni251 – 458208N-acetyltransferaseUniRule annotationAdd
    BLAST

    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.
    OMAiDCVTNQD.
    OrthoDBiEOG6Z6FQZ.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    HAMAPiMF_01631. GlmU.
    InterProiIPR005882. Bifunctional_GlmU.
    IPR001451. Hexapep_transf.
    IPR005835. NTP_transferase.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR011004. Trimer_LpxA-like.
    [Graphical view]
    PfamiPF00132. Hexapep. 2 hits.
    PF00483. NTP_transferase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51161. SSF51161. 1 hit.
    SSF53448. SSF53448. 1 hit.
    TIGRFAMsiTIGR01173. glmU. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A2RMV7-1 [UniParc]FASTAAdd to Basket

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    MNKFAIVLAA GKGTRMKSAL PKVLHQVAGK SMLAHVLKSV SEVEIAKNVV    50
    IVGHEADRVI ATLPKGTQFV KQVEQLGTGH AVRIAADLLA NEEGATLVIA 100
    GDTPLITGET LGALFDYHFA QKATATILTA IAPNPTGYGR IIRDEKDSVE 150
    KIVEQKDANA FEKSITEINT GTYIFDNKSL FKALTEITTD NAQGEYYLTD 200
    VIEIFKKVGQ TIAAHILDDF DESLGVNDRV ALSQAEATMR KRINHEHMVN 250
    GVTLIDPATT YIDSEVTIGA ETVIEANVTI KGNTFIGKNV LITNGSRIEN 300
    SEIHSNCEVR NSTVEESRMS VGSNVGPYAH LRPGTVLSEE VHVGNFVEIK 350
    GSTLGKGTKA GHLTYIGNAT VGEKVNFGAG TITANFDGKN KFNTEIDDFA 400
    FIGSNSTIIA PLHIGKNALT AAGSVVTEDV PDEAVEIGRG KQVNKLGRAK 450
    KMPHYRGQ 458
    Length:458
    Mass (Da):49,122
    Last modified:March 6, 2007 - v1
    Checksum:i316B0BCDDC8F6546
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM406671 Genomic DNA. Translation: CAL98643.1.
    RefSeqiWP_011835789.1. NC_009004.1.
    YP_001033331.1. NC_009004.1.

    Genome annotation databases

    EnsemblBacteriaiCAL98643; CAL98643; llmg_2076.
    GeneIDi4797872.
    KEGGillm:llmg_2076.
    PATRICi22285342. VBILacLac4574_2123.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM406671 Genomic DNA. Translation: CAL98643.1 .
    RefSeqi WP_011835789.1. NC_009004.1.
    YP_001033331.1. NC_009004.1.

    3D structure databases

    ProteinModelPortali A2RMV7.
    SMRi A2RMV7. Positions 2-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 416870.llmg_2076.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL98643 ; CAL98643 ; llmg_2076 .
    GeneIDi 4797872.
    KEGGi llm:llmg_2076.
    PATRICi 22285342. VBILacLac4574_2123.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00532 .
    UPA00113 ; UER00533 .
    UPA00973 .
    BioCyci LLAC416870:GCDT-2078-MONOMER.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    HAMAPi MF_01631. GlmU.
    InterProi IPR005882. Bifunctional_GlmU.
    IPR001451. Hexapep_transf.
    IPR005835. NTP_transferase.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR011004. Trimer_LpxA-like.
    [Graphical view ]
    Pfami PF00132. Hexapep. 2 hits.
    PF00483. NTP_transferase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51161. SSF51161. 1 hit.
    SSF53448. SSF53448. 1 hit.
    TIGRFAMsi TIGR01173. glmU. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
      Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
      J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MG1363.

    Entry informationi

    Entry nameiGLMU_LACLM
    AccessioniPrimary (citable) accession number: A2RMV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 58 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

    Documents

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

    External Data

    Dasty 3