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Q89VX9

- GLND_BRADU

UniProt

Q89VX9 - GLND_BRADU

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (05 Jul 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 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

    BioCyciBJAP224911:GJEJ-925-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:bll0916
    OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
    Taxonomic identifieri224911 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
    ProteomesiUP000002526: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 929929Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192721Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi224911.bll0916.

    Structurei

    3D structure databases

    ProteinModelPortaliQ89VX9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini524 – 59774HDUniRule annotationAdd
    BLAST
    Domaini740 – 82283ACT 1UniRule annotationAdd
    BLAST
    Domaini850 – 92778ACT 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.
    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. 2 hits.
    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.

    Q89VX9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSVTTEHKQ EVDDRFDTAR ITAAVDALAE KHQGREDAFR TAMAQLLKAE    50
    LIAARAAAQA ILLKDRHGRR CAERLCHVQD EIIRILYSAA TRHLYRSPIP 100
    SGAERMAVVA TGGYGRGLMA PESDIDLLFI LPYKQTAWGE QVAEAILYCL 150
    WDMGLKVGHA TRSVDESIRQ ARGDMTIRTA ILETRFLTGD QPLYDELVER 200
    FDKEVVQGTA SEFVTAKLAE REERHRRGGQ SRYLVEPNVK DGKGALRDLH 250
    TLFWIAKYVY RVRDTDELVE RGVFDAQEYR TFRRCADFLW SVRCNLHFYS 300
    GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLV AKEVGNLTAI 350
    LCAKLEDQQA KPAPVLSRMM ARLRPTPAKR RVPDSDDFIV DNNRINVAAP 400
    DVFKHDPVNL IRIFRLAQKH NLAFHPDAMR DVTRSLGLIN AQLRENPEAN 450
    RLFMEILTSD NAEIVLRRMN ETGVLGHFIR AFGKIVSMMQ FNMYHHYTVD 500
    EHLIRCVGFL QDIERGGIEE FAVASDLMRK IRPEHRSVIY IATLLHDVAK 550
    GRPEDHSIAG AKVARRLCPR LGFSPADTEL VAWLIEEHLT MSTVAQSRDL 600
    SDRKTIENFA AVVQSVEQMK LLTILTTADI RGVGPGVWNG WKAQLLRSLY 650
    YETEPVLTGG FSEVDRGKRL TAAYAEFRNA FAEWPADELD AYIARHYPAY 700
    WLKVELPRKI RHARFVRSSE QAGHKLAINV GFDEVRGVTE LTIFAADHPW 750
    LLSIIAGACA SAGANIVDAQ IYTTTDGRAL DTISISREYD RDEDEGRRAT 800
    RIGEMIEDVL EGKLRLPEVV ARRTVRSKAR PFVIEPEVTI NNQWSDRYTV 850
    IEVSGLDRPG LLYELTTAIS KLNLNIASAH VATFGERARD VFYVTDLLGA 900
    QINAPTRQSA IKSALTHVMA GDKAVQPAA 929
    Length:929
    Mass (Da):105,033
    Last modified:July 5, 2004 - v2
    Checksum:iE4A270C497C26D5E
    GO

    Sequence cautioni

    The sequence BAC46181.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000040 Genomic DNA. Translation: BAC46181.1. Different initiation.
    RefSeqiNP_767556.1. NC_004463.1.

    Genome annotation databases

    EnsemblBacteriaiBAC46181; BAC46181; BAC46181.
    GeneIDi1049859.
    KEGGibja:bll0916.
    PATRICi21185328. VBIBraJap65052_0935.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000040 Genomic DNA. Translation: BAC46181.1 . Different initiation.
    RefSeqi NP_767556.1. NC_004463.1.

    3D structure databases

    ProteinModelPortali Q89VX9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224911.bll0916.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC46181 ; BAC46181 ; BAC46181 .
    GeneIDi 1049859.
    KEGGi bja:bll0916.
    PATRICi 21185328. VBIBraJap65052_0935.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BJAP224911:GJEJ-925-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. 2 hits.
    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: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

    Entry informationi

    Entry nameiGLND_BRADU
    AccessioniPrimary (citable) accession number: Q89VX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 72 of the entry and version 2 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