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Q9CNH1

- GLND_PASMU

UniProt

Q9CNH1 - GLND_PASMU

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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

    BioCyciPMUL272843:GC8W-472-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:PM0460
    OrganismiPasteurella multocida (strain Pm70)
    Taxonomic identifieri272843 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
    ProteomesiUP000000809: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 864864Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192749Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272843.PM0460.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CNH1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini447 – 579133HDUniRule annotationAdd
    BLAST
    Domaini687 – 76680ACT 1UniRule annotationAdd
    BLAST
    Domaini793 – 86472ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 328328UridylyltransferaseAdd
    BLAST
    Regioni329 – 686358Uridylyl-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.
    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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF01842. ACT. 2 hits.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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.

    Q9CNH1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLFPYFPLSE LDVSAVRTQK ENLKQFELTQ FAHYEIYDLI TNRTQFCDHL    50
    LRDLWLRFGL VKDNTLTLIA VGGYGREEMF PLSDLDFLIL TSEQVEAQTE 100
    QKIRQFVQFL WDCGFDVGHA VRTLSECEQA GRDNITVATN LLEARYLEGN 150
    FSQFQQLDNV LQKADFWPRE AFFQAKYQER VERYQRYHNT SYNLEPDIKH 200
    SPGGLRDLHL LYWIALRHTG AKNLTDILNS GFIYPQEYAQ LLESQQFLFK 250
    VRFALHLILK RYDNRLLFER QIRVAELLEF VGPGNQGVEK MMKSFFQALQ 300
    TISLLSDLLV KHYREHFLQT NEPVQVRLLD KEFQCVNNAI CLRQANLFVE 350
    QPEQILSLFF HLTQDHQLDI HSSTLRQLHL ALEQRSGYLS ELPVARERFL 400
    RLFNQPGAIA RALVPMHKYG VLKAYLPQWH HIEGLMQFDL FHCYTVDEHI 450
    VRTLLKLEYF LEAESVVPHP ICSQIFSRLT DRTLLYIAAL FHDIAKGRGG 500
    DHAELGAVDV AQFAQQHGFD QREIHTLTWL VEQHLLMSVT AQRRDIHDPE 550
    VVLHFAEAVQ NNVRLDYLTC LTVADICATN ETLWNSWKRT LIATLYQFTT 600
    QQFAQGMDCL LDHAEKIENH RQQALTLLTQ NSLLSAVQIE EIWQHCPEEY 650
    FLRNTPKQIA WHTELLADNQ TELLVKISNR FSEGGTEIFV YCQDQPNLFH 700
    KVVTTIGAKK FSIHDAQIIT SHDGYVFDSF IITELDGKLV KFDRRRSLEK 750
    ALMQALNTSK LPTFRATDNP KLQHFHVKTE VRFLKEQRTD QTEMELFALD 800
    QTGLLAKVSQ VFSELKLNLL NAKITTIGEK AEDFFILTNS EDRALTAEQR 850
    QCLTQRLHEV LEPK 864
    Length:864
    Mass (Da):100,736
    Last modified:June 1, 2001 - v1
    Checksum:i591B1D4F2FA62F4E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK02544.1.
    RefSeqiNP_245397.1. NC_002663.1.
    WP_010906658.1. NC_002663.1.

    Genome annotation databases

    EnsemblBacteriaiAAK02544; AAK02544; PM0460.
    GeneIDi1243807.
    KEGGipmu:PM0460.
    PATRICi22870096. VBIPasMul88067_0472.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK02544.1 .
    RefSeqi NP_245397.1. NC_002663.1.
    WP_010906658.1. NC_002663.1.

    3D structure databases

    ProteinModelPortali Q9CNH1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272843.PM0460.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK02544 ; AAK02544 ; PM0460 .
    GeneIDi 1243807.
    KEGGi pmu:PM0460.
    PATRICi 22870096. VBIPasMul88067_0472.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PMUL272843:GC8W-472-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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view ]
    Pfami PF01842. ACT. 2 hits.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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: Pm70.

    Entry informationi

    Entry nameiGLND_PASMU
    AccessioniPrimary (citable) accession number: Q9CNH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 81 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