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A5ETJ9

- GLND_BRASB

UniProt

A5ETJ9 - GLND_BRASB

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (12 Jun 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 fixation 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 fixation Source: UniProtKB-HAMAP
    2. regulation of nitrogen utilization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Nitrogen fixation

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciBSP288000:GJBR-7337-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:BBta_7648
    OrganismiBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
    Taxonomic identifieri288000 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
    ProteomesiUP000000246: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 931931Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022327Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi288000.BBta_7648.

    Structurei

    3D structure databases

    ProteinModelPortaliA5ETJ9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini523 – 59977HDUniRule annotationAdd
    BLAST
    Domaini740 – 82283ACT 1UniRule annotationAdd
    BLAST
    Domaini851 – 93181ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 383383UridylyltransferaseAdd
    BLAST
    Regioni384 – 739356Uridylyl-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.
    HOGENOMiHOG000261779.
    KOiK00990.
    OMAiHHLLMSV.
    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.

    A5ETJ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSVTPNSRP ESFPEFDSAG LAAAVDALAA QHSGREDMFR AAVVQLLKAE    50
    LVKARAVAQA QLLKDRHGRR CAERLCFVQD EIIRILYAAA TQHLYRSQVP 100
    SGAERMAVVA TGGYGRGLMA PESDIDLLFI LPYKQTAWGE QVAEAILYSL 150
    WDMGLKVGHA TRSVDESIRQ ARGDMTIRTA ILETRYLAGD RPLYDELVER 200
    FDTEVVQGTA AEFVAAKLAE REERHRRGGQ SRYLVEPNVK DGKGGLRDLH 250
    TLFWIAKYVY RVRETAELVE RGVFDAHEYR TFRRCADFLW SVRCNLHFVS 300
    GRPEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLV AKEVGNLTAI 350
    LCAKLEDQQA KPAPVLSRVI SRLKTGNSWR RVPESDDFIV DNNRINLAAP 400
    DVFKHDPVNL IRIFRLAQKN NLAFHPDAMR AVTRSLNLIN TELRDNPDAN 450
    RLFMEILTSN DAETVLRRMN ETGVLGHFIR AFGRIVSMMQ FNMYHHYTVD 500
    EHLIRCIGFL QEIERGGIDE FALASDLMRK IRPEHRAVIY ISVLLHDVAK 550
    GRPEDHSIAG AKVARRLCPR LGFNNADTEL VAWLIEEHLT MSTVAQSRDL 600
    SDRRTIEKFA AVVQSVEQMK LLTILTTADI RGVGPGVWNG WKAQLLRTLY 650
    YETEPVLTGG FSEVNRAKRI TAAQAEFRNA FTDWPEDELN TYIGRHYPAY 700
    WLKVELPRKI RHARFVRASE DAGHKLAINV GFDPARGVTE LTIFAMDHPW 750
    LLSIIAGACA SAGANIVDAQ IYTTTDGRAL DTIAISREYE RDEDEGRRAT 800
    RIGETIEQVL EGKLRLPDAV ARRTTRGKQH KAFSVEPEVS INNQWSELYT 850
    VIEVSGLDRP GLLYELTTAI SKLNLNIASA HVATFGERAR DVFYVTDLLG 900
    AQINAPTRQA AIKSALLHLL ASDDTAAQPA A 931
    Length:931
    Mass (Da):104,895
    Last modified:June 12, 2007 - v1
    Checksum:i2C910DCB195E85E3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000494 Genomic DNA. Translation: ABQ39493.1.
    RefSeqiWP_012047384.1. NC_009485.1.
    YP_001243399.1. NC_009485.1.

    Genome annotation databases

    EnsemblBacteriaiABQ39493; ABQ39493; BBta_7648.
    GeneIDi5149882.
    KEGGibbt:BBta_7648.
    PATRICi21215907. VBIBraSp29847_7601.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000494 Genomic DNA. Translation: ABQ39493.1 .
    RefSeqi WP_012047384.1. NC_009485.1.
    YP_001243399.1. NC_009485.1.

    3D structure databases

    ProteinModelPortali A5ETJ9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 288000.BBta_7648.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ39493 ; ABQ39493 ; BBta_7648 .
    GeneIDi 5149882.
    KEGGi bbt:BBta_7648.
    PATRICi 21215907. VBIBraSp29847_7601.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261779.
    KOi K00990.
    OMAi HHLLMSV.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci BSP288000:GJBR-7337-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: BTAi1 / ATCC BAA-1182.

    Entry informationi

    Entry nameiGLND_BRASB
    AccessioniPrimary (citable) accession number: A5ETJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 53 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