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Q1LNG0

- GLND_RALME

UniProt

Q1LNG0 - GLND_RALME

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (30 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

    BioCyciCMET266264:GJ5G-1494-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:Rmet_1433
    OrganismiRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
    Taxonomic identifieri266264 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000002429: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 857857Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000078810Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi266264.Rmet_1433.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1LNG0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini442 – 544103HDUniRule annotationAdd
    BLAST
    Domaini680 – 76081ACT 1UniRule annotationAdd
    BLAST
    Domaini788 – 85770ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 322322UridylyltransferaseAdd
    BLAST
    Regioni323 – 679357Uridylyl-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.

    Q1LNG0-1 [UniParc]FASTAAdd to Basket

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    MDTTPELLLC QRIRDKLKAD KQVLFAEFDA NNQVNPLVTK LRRAVDVALT    50
    EAWTGLELPG DVALVAVGGY GRGELFPHSD VDVLLLLPGE PDAKMAAKLE 100
    RFIGLCWDLG LEIGSSVRTV DDCIRESAAD ITIRTSLLEA RLLIGNKALF 150
    KSLQTRYQAD MDAADFFQAK LLEMRQRHAK YQDTPYALEP NCKESPGGLR 200
    DLQVILWMTE AARLGDSWKQ LFERGLLTER EAQELTRNER LLRTIRARLH 250
    LLAGRRQDVL VFDLQTALAE AFGYRQTTNK RASEQLMRRY YWAAKAVTQL 300
    NSVLLLNIEA MLFPSESMVT REINDRFVER QGMLEITSDD LYERNPHAIL 350
    ETFLLYERTP GVKGLSPRTL RGLYNARTVM DASWRNDPVN RRLFLAIVQE 400
    PQGITHALRL MNQTSVLGRY LINFRRIVGQ MQHDLFHVYT VDQHILMVVR 450
    NMRRFAIVEH THEFPFCSQL MAGFDRPWVL WVAALFHDIA KGRGGDHSKL 500
    GTVDARRFCK QHGISREDTD LIAWLVEHHL TMSHVAQKQD LTDPDVVKAF 550
    AQVVGNGRYL TALYLLTVAD IRGTSPKVWN AWKGKLLEDL YRITLRVLGG 600
    ARLDTHSLWA QKRDDTIAQL RLKAFDPELA KPLWDKLDMS FFMRQDARDI 650
    AWLTRSLFNK VNSPNPVVKA RISPAGEGLQ VAVYVKDQPD LFARICGYFE 700
    RKAFSIQDAK IETTRDGYAL DTFQITDPGL AGDYRDILTL VEHELGERVR 750
    LECPLPDPTQ GRLSRQSRSF PIKPRVDLRP DERGQYYLLS VSANDRTGLL 800
    YAIARVLAKH RVSVHSARIN TLGERVEDVF LVDGSRLAAD NRLQIQLEQD 850
    LLDALAI 857
    Length:857
    Mass (Da):97,774
    Last modified:May 30, 2006 - v1
    Checksum:i0BFF1E5B9F7498A8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000352 Genomic DNA. Translation: ABF08316.1.
    RefSeqiWP_011516184.1. NC_007973.1.
    YP_583585.1. NC_007973.1.

    Genome annotation databases

    EnsemblBacteriaiABF08316; ABF08316; Rmet_1433.
    GeneIDi4038236.
    KEGGirme:Rmet_1433.
    PATRICi20287480. VBIRalMet4734_1842.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000352 Genomic DNA. Translation: ABF08316.1 .
    RefSeqi WP_011516184.1. NC_007973.1.
    YP_583585.1. NC_007973.1.

    3D structure databases

    ProteinModelPortali Q1LNG0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266264.Rmet_1433.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABF08316 ; ABF08316 ; Rmet_1433 .
    GeneIDi 4038236.
    KEGGi rme:Rmet_1433.
    PATRICi 20287480. VBIRalMet4734_1842.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CMET266264:GJ5G-1494-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: CH34 / ATCC 43123 / DSM 2839.

    Entry informationi

    Entry nameiGLND_RALME
    AccessioniPrimary (citable) accession number: Q1LNG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 64 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