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A2SB69

- GLND_BURM9

UniProt

A2SB69 - GLND_BURM9

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Burkholderia mallei (strain NCTC 10229)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      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

    BioCyciBMAL412022:GJI8-3251-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:BMA10229_A3252
    OrganismiBurkholderia mallei (strain NCTC 10229)
    Taxonomic identifieri412022 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000002283: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 858858Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022332Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi412022.BMA10229_A3252.

    Structurei

    3D structure databases

    ProteinModelPortaliA2SB69.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini444 – 550107HDUniRule annotationAdd
    BLAST
    Domaini682 – 76180ACT 1UniRule annotationAdd
    BLAST
    Domaini790 – 85869ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 324324UridylyltransferaseAdd
    BLAST
    Regioni325 – 681357Uridylyl-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.

    A2SB69-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSASVAEPPP ALSRKAEFKA AKAELLARFK SANHVTPLMH ALSRATDDAL    50
    RSLWQECGLP ATLALVAVGG FGRGELSPHS DVDILVLLPD AHASELDERI 100
    ERFIGMAWDL GLEIGSSVRT VDQCIEEASH DVTVQTSLLE ARRIVGSTAL 150
    FERFMLRYRE ALDARAFFQA KVLEMRQRHA KFQDTPYSLE PNVKESPGGL 200
    RDLQTILWIA RAAGFGSSWR ELDTRGLITD REARELRRNE GFLKTLRARL 250
    HVIAGRRQDI LVFDLQTQAA ESFGYQPTSA KRASEQLMRR YYWAAKAVTQ 300
    LATILIQNIE AQLFPATSGV TRVLSPGRFV EKQGMLEIAA DDVFERHPDA 350
    ILEAFLLYEA TRGVKGLSAR TLRALYNSRD VMNNAWRRDP RNRHTFMQIL 400
    QQPEGITHAF RLMNQTSVLG RYLLNFRRIV GQMQHDLYHV YTVDQHILMV 450
    LRNIRRFAVA EHAHEYPFCS QLIVNFERPW VLYVAALFHD IAKGRGGDHS 500
    ALGMADARRF CREHGIEGDD AALVVWLVQH HLTMSQVAQK QDTSDPVVIK 550
    RFAELVGSER RLTALYLLTV ADIRGTSPKV WNTWKGKLLE DLYRATLAVL 600
    GGAQPDAHSE LKTRQEEALA LLRLETVPPD AHRALWDQLD VGYFLRHDAA 650
    DIAWQTRVLY RHVAADTAIV RARPSPVGDA LQVLVYVKDR SDLFAGICAY 700
    FDRNGLSVLD ARVNTTRHGY ALDNFIVTQT EHDVQYRDIA NLVEQQLAAR 750
    LAESAPLPEP SKGRLSRLSR TFPITPRVDL RADERGQYYI LSVSANDRPG 800
    LLYSIARVLA EHRVGVHAAR INTLGERVED VFMLDGTGLS DNRLQIQVET 850
    ELLRAIAV 858
    Length:858
    Mass (Da):96,750
    Last modified:March 6, 2007 - v1
    Checksum:iE71C618DBA6FE7F4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000546 Genomic DNA. Translation: ABN00892.1.
    RefSeqiYP_001029188.1. NC_008836.1.

    Genome annotation databases

    EnsemblBacteriaiABN00892; ABN00892; BMA10229_A3252.
    GeneIDi4793516.
    KEGGibml:BMA10229_A3252.
    PATRICi19137520. VBIBurMal46188_5445.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000546 Genomic DNA. Translation: ABN00892.1 .
    RefSeqi YP_001029188.1. NC_008836.1.

    3D structure databases

    ProteinModelPortali A2SB69.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 412022.BMA10229_A3252.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN00892 ; ABN00892 ; BMA10229_A3252 .
    GeneIDi 4793516.
    KEGGi bml:BMA10229_A3252.
    PATRICi 19137520. VBIBurMal46188_5445.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BMAL412022:GJI8-3251-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. DeShazer D., Woods D.E., Nierman W.C.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCTC 10229.

    Entry informationi

    Entry nameiGLND_BURM9
    AccessioniPrimary (citable) accession number: A2SB69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 56 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