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Q5WVX6

- GLND_LEGPL

UniProt

Q5WVX6 - GLND_LEGPL

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Legionella pneumophila (strain Lens)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    Functioni

    Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.UniRule annotation

    Catalytic activityi

    UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
    Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Enzyme regulationi

    Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.UniRule annotation

    GO - Molecular functioni

    1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
    2. amino acid binding Source: InterPro
    3. metal ion binding Source: InterPro
    4. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. nitrogen compound metabolic process Source: InterPro
    2. regulation of nitrogen utilization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciLPNE297245:GJD4-1810-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
    Short name:
    UTase/URUniRule annotation
    Alternative name(s):
    Bifunctional [protein-PII] modification enzymeUniRule annotation
    Bifunctional nitrogen sensor proteinUniRule annotation
    Including the following 2 domains:
    [Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
    Short name:
    PII uridylyltransferaseUniRule annotation
    Short name:
    UTaseUniRule annotation
    [Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
    Short name:
    URUniRule annotation
    Gene namesi
    Name:glnDUniRule annotation
    Ordered Locus Names:lpl1684
    OrganismiLegionella pneumophila (strain Lens)
    Taxonomic identifieri297245 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
    ProteomesiUP000002517: Chromosome

    Organism-specific databases

    LegioListilpl1684.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 861861Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192740Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi297245.lpl1684.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5WVX6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini441 – 569129HDUniRule annotationAdd
    BLAST
    Domaini679 – 76082ACT 1UniRule annotationAdd
    BLAST
    Domaini788 – 86174ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 321321UridylyltransferaseAdd
    BLAST
    Regioni322 – 678357Uridylyl-removingAdd
    BLAST

    Domaini

    Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.UniRule annotation

    Sequence similaritiesi

    Belongs to the GlnD family.UniRule annotation
    Contains 2 ACT domains.UniRule annotation
    Contains 1 HD domain.UniRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG2844.
    HOGENOMiHOG000261778.
    KOiK00990.
    OMAiHHLLMSV.
    OrthoDBiEOG6CCH44.

    Family and domain databases

    Gene3Di1.10.3210.10. 1 hit.
    HAMAPiMF_00277. PII_uridylyl_transf.
    InterProiIPR002912. ACT_dom.
    IPR010043. GlnD_Uridyltrans.
    IPR005105. GlnD_Uridyltrans_N.
    IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF03445. DUF294. 1 hit.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
    SMARTiSM00471. HDc. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
    PROSITEiPS51671. ACT. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5WVX6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNDNRIIKN TIKQFKEKLC RDFSQKANIT SITRKLAVFI DTILIQLFIK    50
    NKLHFGDNFC LLALGSYGRR ELQLHSDIDL LILHTEKVSN IQLQRAQKFI 100
    QDCWDVGLEV SHQITTVSSC ANLASQDLSV ISTIMDMFLL CGHGALMEEL 150
    IYQTHTLHMW PSHQYFFAKL QEQQSRYAKY GETAYNLEPN IKNGPGGLRD 200
    LQILLSISKR HFKIKKLAEG IGYGFITDKE YEELKYCQNF LWRVRFALHM 250
    LAGKPEERLS FDYQVKLAQF FGYQDQSHIL AIEQFMKDYF KVIKRNRELN 300
    EMLLQWFNET IVYHQKQKII RLDDEFQLSN RFIEVRNNRV FKQNPQSILK 350
    LFYWLVKRPD IEGVRASTIR LIRESLFLMG KRFRESKETA NIFVNIFRTG 400
    NDPYDALQRM NRYGVLAHYL DCFATVTGQM QYDLFHAYTV DQHTLFVIRN 450
    ISRFKKNEYA KQFPLCAKII TALEKPEILY LGALFHDIAK GRGGDHSELG 500
    AIEAQQFTQR HYMEAEDSKL IVWLVRYHLL MSQTAQRKDI YDPKTIEQFC 550
    QLLPHAKYLD YLYLLTVADI CGTNPTLWNA WKDSLLKELY HAAKTRLHKQ 600
    QELLDEAALI SIRKQYAMDI LISDGISSRV IQDLWSQFKG KYFLHESPEV 650
    IARHTKAILN SKQFPVVIIM PHHSQGGTEV FIYMPHKDER FTITTSVLSN 700
    HHVTIQEAAI ITCDNQFDLD TYIILDENNQ AFLNEQRARD IQKSLCDHLA 750
    NTGRLPAVSR RRLSRALTHF NVKTQINFID DNTNHQTQLF LVTNDRPGLL 800
    ATISRVFLTL NIHLHNAKIA TAGERVEDMF YISNQTGYSL NHEEKTILKE 850
    KLILEISKSK Y 861
    Length:861
    Mass (Da):100,671
    Last modified:November 23, 2004 - v1
    Checksum:i4D1AB5D391DCE105
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628337 Genomic DNA. Translation: CAH15924.1.
    RefSeqiYP_127023.1. NC_006369.1.

    Genome annotation databases

    EnsemblBacteriaiCAH15924; CAH15924; lpl1684.
    GeneIDi3113365.
    KEGGilpf:lpl1684.
    PATRICi22317079. VBILegPne33733_1866.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628337 Genomic DNA. Translation: CAH15924.1 .
    RefSeqi YP_127023.1. NC_006369.1.

    3D structure databases

    ProteinModelPortali Q5WVX6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 297245.lpl1684.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH15924 ; CAH15924 ; lpl1684 .
    GeneIDi 3113365.
    KEGGi lpf:lpl1684.
    PATRICi 22317079. VBILegPne33733_1866.

    Organism-specific databases

    LegioListi lpl1684.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261778.
    KOi K00990.
    OMAi HHLLMSV.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci LPNE297245:GJD4-1810-MONOMER.

    Family and domain databases

    Gene3Di 1.10.3210.10. 1 hit.
    HAMAPi MF_00277. PII_uridylyl_transf.
    InterProi IPR002912. ACT_dom.
    IPR010043. GlnD_Uridyltrans.
    IPR005105. GlnD_Uridyltrans_N.
    IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view ]
    Pfami PF03445. DUF294. 1 hit.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006288. PII_uridyltransf. 1 hit.
    SMARTi SM00471. HDc. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01693. UTase_glnD. 1 hit.
    PROSITEi PS51671. ACT. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
      Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
      Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Lens.

    Entry informationi

    Entry nameiGLND_LEGPL
    AccessioniPrimary (citable) accession number: Q5WVX6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 23, 2004
    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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3