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A5VN81

- GLND_BRUO2

UniProt

A5VN81 - GLND_BRUO2

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (10 Jul 2007)
      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

    BioCyciBOVI444178:GH2V-138-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:BOV_0139
    OrganismiBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
    Taxonomic identifieri444178 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000006383: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 934934Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022329Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi444178.BOV_0139.

    Structurei

    3D structure databases

    ProteinModelPortaliA5VN81.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini497 – 613117HDUniRule annotationAdd
    BLAST
    Domaini737 – 81882ACT 1UniRule annotationAdd
    BLAST
    Domaini848 – 93184ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 379379UridylyltransferaseAdd
    BLAST
    Regioni380 – 736357Uridylyl-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.
    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. 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.

    A5VN81-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAHDLKLEE IVNAETLRRK LNELADTADE SYTSLPMRKV VLQTLKDALA    50
    SGRANAEDML MKDGGGTLCA KRLCYLMDTL IDILFEFATT RAYPTRNPSK 100
    AENMALVAVG GYGRGGLAQG SDIDLLFLLP YKQTPWGEQV VEYTLYMLWD 150
    MGLKVGHSTR NIDECIRLAR EDMTIRTALL DARFLTGDKD LFRTLEIRFE 200
    EEIVKGTEPE FIQAKLAERD ARHRKAGETR YLVEPNVKEG KGGQRDLHTL 250
    FWITKYFYRV KTKEELVKLG VLSRAELKLF NKAEDFLWAV RCHMHFATLK 300
    AEERLSFDIQ PEIAQRLGYT AHPGQNYVER FIKHYFLVAK DVGDLTRIIC 350
    AALEEQQAKH VPGFNRIFLT FSRRKRKLSD DGAFISENHR INIARPDIFR 400
    QDPVNMIRLF HLADRHGLEF HPEAMQSLTR SLKLINADLR ENPEANRLFL 450
    EILTSPRNPE LILRRMNESG VLGKFIPDFG KIVAMMQFNM YHHYTVDEHL 500
    LRCIAVLSEI EHGELKTEHP LSNHLITTIK RDRNLLYVTL LLHDIAKGRP 550
    EDHSIAGARI ARRLCPRFGL TPSETETVEW LVREHLTMSM VAQSRDLNDR 600
    KTIIDFADTV QTMERLKLLL ILTVCDIKAV GPGIWNGWKG QLLRTLFYET 650
    ELVLTGGFSE LSRAARDKQA REALAERLSD WPKEERDAYL ALPYTNYFLT 700
    VSLDDQVRHA HFIRDADQQG RALVTMAKPH AFEAVTEITV LAPDHPRLLS 750
    VITGACAAAG GNIVDAQIFT TSDGRALDTI LISREFDTDD DERRQAERVG 800
    KVIEDVLSGK AHLPDMLAKR TKPKKAARAF KVEPRVEINN TLSNKFTVIE 850
    VEGLDRPGLL SELTGLISDL SLDIASAHIT TFGEKVIDSF YVTDLVGHKI 900
    SNATRQGNIK RKLLALLGAE NGARTNGRSP QAAA 934
    Length:934
    Mass (Da):105,884
    Last modified:July 10, 2007 - v1
    Checksum:i5CAFF6DB710AB78A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000708 Genomic DNA. Translation: ABQ61661.1.
    RefSeqiYP_001258178.1. NC_009505.1.

    Genome annotation databases

    EnsemblBacteriaiABQ61661; ABQ61661; BOV_0139.
    GeneIDi5202925.
    KEGGibov:BOV_0139.
    PATRICi17859996. VBIBruOvi136990_1422.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000708 Genomic DNA. Translation: ABQ61661.1 .
    RefSeqi YP_001258178.1. NC_009505.1.

    3D structure databases

    ProteinModelPortali A5VN81.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 444178.BOV_0139.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ61661 ; ABQ61661 ; BOV_0139 .
    GeneIDi 5202925.
    KEGGi bov:BOV_0139.
    PATRICi 17859996. VBIBruOvi136990_1422.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BOVI444178:GH2V-138-MONOMER.

    Miscellaneous databases

    PROi A5VN81.

    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. Paulsen I.
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25840 / 63/290 / NCTC 10512.

    Entry informationi

    Entry nameiGLND_BRUO2
    AccessioniPrimary (citable) accession number: A5VN81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 53 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