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Q5LWE5

- GLND_RUEPO

UniProt

Q5LWE5 - GLND_RUEPO

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Feb 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

    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:SPO0397
    OrganismiRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
    Taxonomic identifieri246200 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
    ProteomesiUP000001023: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 908908Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192769Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi246200.SPO0397.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5LWE5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini478 – 598121HDUniRule annotationAdd
    BLAST
    Domaini719 – 80183ACT 1UniRule annotationAdd
    BLAST
    Domaini829 – 90476ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 360360UridylyltransferaseAdd
    BLAST
    Regioni361 – 718358Uridylyl-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. 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.

    Q5LWE5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFDTPAVFAR ITEAAAEAAD NAALRGAVVA ILRDVQNAGR AAIAEGFAED    50
    PFAARPLTRA YTYLTDGMVK TAMYVASEIL HPLATPTQGE RIAVLAVGGF 100
    GRGEMAPFSD VDLLFLTPYK ITAWAESVIE SMLYILWDLR LKVGHSSRTV 150
    KDCIRLGRDD FTIRTAMLEH RFLAGHAPLA RSLDQRLKSE LYKDTQREFI 200
    EAKLEERDAR HRKQGERYMV EPNVKEGKGG LRDLQSLYWI AKYIYEVKET 250
    AELVPLGLFT PSEYRTFVQA EEFLWAVRAH LHLVTGRATE QLTFDLQVEV 300
    AARMGYQDRA GRRGVEVFMQ KYFREATRVG ELTRIFLTKL EAAHMKGAPL 350
    LERIFRRRRR IKQGYKVVRG RLDVVDPEAF LADKLNLLRI FEEALRTGML 400
    IHPDAMRLVT ANLDLIDDGM RNDKEARRIF LDLLLKHGNP ERALRRMNEL 450
    GVLSAFVPEF EPIVAMMQFN MYHSYTVDEH TIQTIVNLAQ IEKGELVESL 500
    PLASSILKAG VNRKVLYVAL LLHDIGKGRP EDHSILGARI ARKVAPRLGL 550
    SKADCETVEW LVRYHLLMSD MAQKRDISDP RTVRDFAKAV QTTKRLDLLT 600
    VLTVCDIRGV GPNTWNNWKA TLLRALHAET KRALEMGMEA LNREGRGNEA 650
    KKALRTALSD WPAGEVKTEI ARHYPPYWQG FNVETHVTFA EMLRQLEHSG 700
    DPGGIEIRLD PDEDRDATRA CFAMADHPGI FSRMAGALAL VGANVVDARS 750
    YTTKDGYVTD AFWIQDAEGH PYEAARLPRL SQMILKTLKG EVVARDALKS 800
    RDKIKKREKA FNVPTHITFD NEGSDIYTII EVDTRDRPGL LYDLARALAA 850
    ANVYIANAVI ATYGEQVVDS FYVKDMFGLK YHSEAKQRTL ETKLRKAITE 900
    GAERAAAS 908
    Length:908
    Mass (Da):102,501
    Last modified:February 1, 2005 - v1
    Checksum:iAA6C869FD08E01F5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000031 Genomic DNA. Translation: AAV93715.1.
    RefSeqiYP_165660.1. NC_003911.12.

    Genome annotation databases

    EnsemblBacteriaiAAV93715; AAV93715; SPO0397.
    GeneIDi3195406.
    KEGGisil:SPO0397.
    PATRICi23374055. VBIRuePom114501_0404.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000031 Genomic DNA. Translation: AAV93715.1 .
    RefSeqi YP_165660.1. NC_003911.12.

    3D structure databases

    ProteinModelPortali Q5LWE5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 246200.SPO0397.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV93715 ; AAV93715 ; SPO0397 .
    GeneIDi 3195406.
    KEGGi sil:SPO0397.
    PATRICi 23374055. VBIRuePom114501_0404.

    Phylogenomic databases

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

    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: ATCC 700808 / DSM 15171 / DSS-3.

    Entry informationi

    Entry nameiGLND_RUEPO
    AccessioniPrimary (citable) accession number: Q5LWE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 73 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