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Q470D5

- GLND_CUPPJ

UniProt

Q470D5 - GLND_CUPPJ

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      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

    BioCyciCPIN264198:GIW3-1903-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:Reut_A1883
    OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
    Taxonomic identifieri264198 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000002697: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 869869Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231689Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi264198.Reut_A1883.

    Structurei

    3D structure databases

    ProteinModelPortaliQ470D5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini451 – 54898HDUniRule annotationAdd
    BLAST
    Domaini689 – 77385ACT 1UniRule annotationAdd
    BLAST
    Domaini800 – 86970ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 331331UridylyltransferaseAdd
    BLAST
    Regioni332 – 688357Uridylyl-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.
    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.

    Q470D5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPTNLPALPM DTTPELLLAA RVRDQLKADK QALFADFDLS SHVGTLVTRL    50
    RRAVDAALAE AWRGLDMPAD AALVAVGGYG RGELFPYSDV DVLLLLRAEP 100
    DADTVSRLER FIGMCWDLGL EIGSSVRTVE DCIREARADI TIQTSLLEAR 150
    LLTGNRKLFE ALRTQHQADL DPAAFFQAKL LEMRQRHAKY QDTPYALEPN 200
    CKESPGGLRD LQVILWMTKA AGLGDSWKEL FERGLLTQRE AQELSRNERL 250
    LKTIRARLHL VAGRRQDVLV FDLQTALAES FGYRQNANKR ASEQLMRRYF 300
    WAAKAVTQLN SVLLLNIEAL LFPSESQVTR VINERFVERQ GMLEITSDSL 350
    YEDDPHAILE TFLLYERTPG IKGLSPRTLR GLYNARTVMD ARWRSDPENR 400
    RLFLAILQEP QGITHALRLM NQTSVLGRYL INFRRIVGQM QHDLFHVYTV 450
    DQHILMVVRN MRRFAIVEHT HEFPFCSQLM ASFDKPWVLS VAALFHDIAK 500
    GRGGDHSKLG TVDARRFCKQ HGIGREDADL ICWLVEHHLT MSHVAQKQDL 550
    TDPDVVHAFA RVVGDERHLT ALYLLTVADV RGTSPKVWNA WKGKLLEDLY 600
    RITLRVLGGA RVDPHSIWAQ RQEETISQLR LKAFDPELGK PLWAQLDVAF 650
    FLRHDSRDIA WLTRHLFNKV DSPVPVVKAR ISPAGEGLQV AVYVKDQPDL 700
    FARICGYFER KAFSIQDAKI HTTRHGYALD TFQVTDPGLA DDGGNYRDIL 750
    ALVEHELGDR LQQQAALPEP SQGRLSRQSR SFPIKPRVDL RPDERGQYYL 800
    LSLSANDRTG LLYAITRVLA KHRVSVHTAR INTLGERVED VFLVDGSRLA 850
    ADNRLQIQLE QDLLAALEI 869
    Length:869
    Mass (Da):98,722
    Last modified:September 13, 2005 - v1
    Checksum:i8028D86E94BE91AE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000090 Genomic DNA. Translation: AAZ61248.1.
    RefSeqiYP_296092.1. NC_007347.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ61248; AAZ61248; Reut_A1883.
    GeneIDi3609562.
    KEGGireu:Reut_A1883.
    PATRICi20229317. VBIRalEut24049_2517.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000090 Genomic DNA. Translation: AAZ61248.1 .
    RefSeqi YP_296092.1. NC_007347.1.

    3D structure databases

    ProteinModelPortali Q470D5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 264198.Reut_A1883.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ61248 ; AAZ61248 ; Reut_A1883 .
    GeneIDi 3609562.
    KEGGi reu:Reut_A1883.
    PATRICi 20229317. VBIRalEut24049_2517.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CPIN264198:GIW3-1903-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. "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JMP134 / LMG 1197.

    Entry informationi

    Entry nameiGLND_CUPPJ
    AccessioniPrimary (citable) accession number: Q470D5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 63 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