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Q2L165

- GLND_BORA1

UniProt

Q2L165 - GLND_BORA1

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Bordetella avium (strain 197N)
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 (07 Mar 2006)
      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

    BioCyciBAVI360910:GCKI-1759-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:BAV1732
    OrganismiBordetella avium (strain 197N)
    Taxonomic identifieri360910 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
    ProteomesiUP000001977: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 858858Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022326Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi360910.BAV1732.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2L165.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini438 – 550113HDUniRule annotationAdd
    BLAST
    Domaini675 – 75682ACT 1UniRule annotationAdd
    BLAST
    Domaini789 – 85870ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 318318UridylyltransferaseAdd
    BLAST
    Regioni319 – 674356Uridylyl-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.

    Q2L165-1 [UniParc]FASTAAdd to Basket

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    MNPTDLHPIK ERMQAARAAA IADFRQHLRP DPLLSELRRI VDQALRDLLK    50
    LCPLPAGATL AAVGGYGRGE LYPHSDVDLL ILLPRAPDGP DESAIETLVA 100
    SLWDLGLEPG HSVRTLAECE TEASADITVE TALLESRWLA GSRSLMKQFE 150
    TAMTARLDAR AFFRAKRVEM QQRHARYQDT PYALEPNSKE SPGGLRDLQV 200
    ILWMARAAGF GRNWRAVAQA GLLTAPEARD LRRAEQAFKR LRIELHLLTR 250
    RREDRLLFDL QPTLAEVYGI ATTTTRRASE LLMQRYYWAA RLVTQLNVIL 300
    IQNIEERLFP RPESDARAID EEFRSLHGRL DIIREDCFER NPTLLLRAFL 350
    VMQQHPGLSG MSARTLRAIW HSRHRIDAQF RRNPVNRKLF LQILQQPRGI 400
    VHELRRMTML NILPRYLPVF RRIVGQMQHD LFHVYTVDQH TLAVIRNLRR 450
    FTMPEHASEY PLASQVMAGL DRHWLLYVAA LFHDIAKGRG GDHSELGARD 500
    ARRFAQEHGL APEDAELVEF LVRQHLLMSA VAQKRDLSDP EVINEFARQV 550
    KDERHLNALY LLTVADIRGT SPKVWNAWKG KLLEDLYRLT LAALGGAQDT 600
    RTVLAERKEE AARLLRLAGL RDDARDAFWQ QLDVAYFLRH DASEIAWHTR 650
    HLYYQVQPDK PVVKVRPTEE GSGLQIMVYT RDTPDLFMNT CAYFDGKAFS 700
    IQDARIHTTR QGWALDSFIV LPAEPLADLR AQAALVEHEL AERLRQAQGG 750
    ARLADVRVFH RNRQSRVSRV FPVMPQAELH PDERSQSWRL SVTATDRPGL 800
    LHALARVMAE NGVNLIMAKI MTLGDRVEDV FIISGAVLER PRTQMQFEHA 850
    VLDALAGE 858
    Length:858
    Mass (Da):97,978
    Last modified:March 7, 2006 - v1
    Checksum:iDE261EA92F0D5AB7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM167904 Genomic DNA. Translation: CAJ49340.1.
    RefSeqiYP_786250.1. NC_010645.1.

    Genome annotation databases

    GeneIDi6266904.
    KEGGibav:BAV1732.
    PATRICi21129646. VBIBorAvi43433_1744.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM167904 Genomic DNA. Translation: CAJ49340.1 .
    RefSeqi YP_786250.1. NC_010645.1.

    3D structure databases

    ProteinModelPortali Q2L165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 360910.BAV1732.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6266904.
    KEGGi bav:BAV1732.
    PATRICi 21129646. VBIBorAvi43433_1744.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BAVI360910:GCKI-1759-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. "Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
      Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
      J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 197N.

    Entry informationi

    Entry nameiGLND_BORA1
    AccessioniPrimary (citable) accession number: Q2L165
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: March 7, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3