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Q7VYD2

- GLND_BORPE

UniProt

Q7VYD2 - GLND_BORPE

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      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

    BioCyciBPER257313:BP1417-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:BP1417
    OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
    Taxonomic identifieri257313 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
    ProteomesiUP000002676: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 865865Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192720Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi257313.BP1417.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7VYD2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini438 – 544107HDUniRule annotationAdd
    BLAST
    Domaini676 – 76287ACT 1UniRule annotationAdd
    BLAST
    Domaini789 – 86577ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 318318UridylyltransferaseAdd
    BLAST
    Regioni319 – 675357Uridylyl-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.
    OMAiLYCLWDM.
    OrthoDBiEOG6CCH44.

    Family and domain databases

    Gene3Di1.10.3210.10. 1 hit.
    HAMAPiMF_00277. PII_uridylyl_transf.
    InterProiIPR002912. ACT_dom.
    IPR010043. GlnD_Uridyltrans.
    IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR002934. Nucleotidyltransferase.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF01842. ACT. 1 hit.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 1 hit.
    PF01909. NTP_transf_2. 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.

    Q7VYD2-1 [UniParc]FASTAAdd to Basket

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    MPHVDLNPLK QRMQAARAAA VAQFRQHPRP DMLLTELRRI VDQALRELVK    50
    LCPLPAGATL AAVGSYGRGE LYPHSDVDLL ILLPQPPSAA DARAVEALVA 100
    ALWDLGLEPG HSVRTLEDCE REARGDITVE TALLESRWLA GSRTLMKRLD 150
    SAMQARLDAA VFFQAKRVEM QQRHAHYQDT PYALEPNCKE SPGGLRDLQV 200
    ILWMARAAGF GHSWREVAQA GLLTSSEARD LRRAEQAFKR LRIELHLLTG 250
    RREDRVLFDL QPGLAAVYGI ASTATRRASE LLMQRYYWAA RLVTQLNVIL 300
    VQNIEERLFP RPDSDARLID DDFRNLRERL DIVREDGFER NPTLLLRAFL 350
    VMQQHPELIG MSARTLRAIW HSRHRIDAQF RRNPVNRKLF LQILQQPRGI 400
    VHELRRMTML NILPRYLPVF RRIVGQMQHD LFHVYTVDQH TLAVVRNLRR 450
    FTMPEHAQEY PLASQLIAGL DRHWLLYVAA LFHDIAKGRG GDHSELGARE 500
    VRRFAQDHGL DPTDAELVEF LVRHHLLMSA VAQKRDLSDP QVVRDFAAQV 550
    GDERRLAALY LLTVADIRGT SPRVWNAWKG KLLEDLFRLT LAALGGAHAD 600
    AHTVLTERKD EAARLTRLAG LRDDAREAFW NQLDIAYFLR HDASEIAWHT 650
    RHLYYQVAPD EPVVRVRPTE HGEGLQVMVY TRDAPDLFVT TCGYFDAKSL 700
    SVQDARVHTT RHGWALDSFI VLAPEGFADL RAQATLVEHE LAERLRDPHA 750
    ARHAHAPRRL PHSHARRSRV FPVMPQAELS PDERSQSWRL SVTATDRPGL 800
    LYALARVFAE HGVDLIMAKI MTLGERVEDV FIVSGSALER PRSQMQFERA 850
    ILDALAGDEP RQQAA 865
    Length:865
    Mass (Da):98,524
    Last modified:October 1, 2003 - v1
    Checksum:iD8E17E5527129A45
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX640415 Genomic DNA. Translation: CAE41707.1.
    RefSeqiNP_880159.1. NC_002929.2.

    Genome annotation databases

    EnsemblBacteriaiCAE41707; CAE41707; BP1417.
    GeneIDi2667683.
    KEGGibpe:BP1417.
    PATRICi21156046. VBIBorPer7866_1519.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX640415 Genomic DNA. Translation: CAE41707.1 .
    RefSeqi NP_880159.1. NC_002929.2.

    3D structure databases

    ProteinModelPortali Q7VYD2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 257313.BP1417.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE41707 ; CAE41707 ; BP1417 .
    GeneIDi 2667683.
    KEGGi bpe:BP1417.
    PATRICi 21156046. VBIBorPer7866_1519.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BPER257313:BP1417-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.
    IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR002934. Nucleotidyltransferase.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view ]
    Pfami PF01842. ACT. 1 hit.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 1 hit.
    PF01909. NTP_transf_2. 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. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
      Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
      , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
      Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

    Entry informationi

    Entry nameiGLND_BORPE
    AccessioniPrimary (citable) accession number: Q7VYD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 70 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3