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Q1QRM1

- GLND_NITHX

UniProt

Q1QRM1 - GLND_NITHX

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Nitrobacter hamburgensis (strain X14 / DSM 10229)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (16 May 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

    BioCyciNHAM323097:GHP7-230-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:Nham_0226
    OrganismiNitrobacter hamburgensis (strain X14 / DSM 10229)
    Taxonomic identifieri323097 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
    ProteomesiUP000001953: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 931931Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022348Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi323097.Nham_0226.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1QRM1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini500 – 59798HDUniRule 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.
    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. 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.

    Q1QRM1-1 [UniParc]FASTAAdd to Basket

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    MDLATTNDAA GAGNDFDTAR ITGDIDALAA KHAGHEDVFR AAVSRLLKAE    50
    LAKVRDAAQA KLLRDRHGRR CAERLCFIQD EIIRLSFSAA TRHLYHSPIP 100
    SDGERMAVVA TGGYGRGLMA PESDIDLLFI LPYKQTAWGE QVAEAILYCL 150
    WDMGLNVGHA TRSVNESIRQ ARRDMTVRTG ILETRFLAGD RALYDELVTR 200
    FDTEVVQGTA AEFVTAKLAE REERHRRAGQ SRYLVEPNVK DGKGGLRDLH 250
    TLFWIAKYVY RVHESRELLG CGVFDVREYR TFRRCADFLW SVRCNLHFAT 300
    GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLT AKDVGDLTAI 350
    LCAKLEDQQA KPAPVLGRMM SRRRPGTELR RVPEGDDFII DNNRINLAAP 400
    DVFKRDPVNL IRVFRLAQKN NLAFHPDALR TVTRSRRLIN AQLRENPEAN 450
    RLFMEILTSN DAETVLRRMN ETGVLGHFIR AFGKIVSMMQ FNMYHHYTVD 500
    EHLLRCIGIL QDIERGGNDE LALASELMRK IHPEHRPVIY ITTLLHDIAK 550
    GRPEDHSIAG ARVARRLCPR LGFNASDTEL IAWLIEQHLT MSKVAQSRDL 600
    SDRKTIENFA AVVQSVEQMK LLTILTTADI RGVGPGVWNG WKAQLLRTLY 650
    YETEPVLTGG FSEVNRVQRI AEAQAEFRAA FTEWSEPELN AYIARHYPAY 700
    WLKVDLAHKI RHARFLRASE QGGRKLNINV GFDEARGVTE LTIFAADHPW 750
    LLSIIAGACA SAGANIVDAQ IYTTTDGQAL DTIAISREYD RDEDEGRRAA 800
    RIGEIIEQVI DGRLRLPDVV ARRAAGKTRL RPFVVEPKVI VNNQWSDRHT 850
    VIEVSGLDRP GLLFQLTAAI SKLNLNIASA HVATFGERAR DVFYVTDLLG 900
    ARITAPTRQA AIKRALIHLL ANGGAAEQSV G 931
    Length:931
    Mass (Da):104,795
    Last modified:May 16, 2006 - v1
    Checksum:i4609DB25262D4648
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000319 Genomic DNA. Translation: ABE61126.1.
    RefSeqiWP_011508832.1. NC_007964.1.
    YP_575586.1. NC_007964.1.

    Genome annotation databases

    EnsemblBacteriaiABE61126; ABE61126; Nham_0226.
    GeneIDi4030820.
    KEGGinha:Nham_0226.
    PATRICi22687799. VBINitHam61822_0939.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000319 Genomic DNA. Translation: ABE61126.1 .
    RefSeqi WP_011508832.1. NC_007964.1.
    YP_575586.1. NC_007964.1.

    3D structure databases

    ProteinModelPortali Q1QRM1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 323097.Nham_0226.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE61126 ; ABE61126 ; Nham_0226 .
    GeneIDi 4030820.
    KEGGi nha:Nham_0226.
    PATRICi 22687799. VBINitHam61822_0939.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci NHAM323097:GHP7-230-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: X14 / DSM 10229.

    Entry informationi

    Entry nameiGLND_NITHX
    AccessioniPrimary (citable) accession number: Q1QRM1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 62 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