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B8GWX0

- GLND_CAUCN

UniProt

B8GWX0 - GLND_CAUCN

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Caulobacter crescentus (strain NA1000 / CB15N)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (03 Mar 2009)
      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

    BioCyciCAULONA1000:CCNA_00013-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:CCNA_00013
    OrganismiCaulobacter crescentus (strain NA1000 / CB15N)
    Taxonomic identifieri565050 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
    ProteomesiUP000001364: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 940940Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000132527Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi190650.CC_0013.

    Structurei

    3D structure databases

    ProteinModelPortaliB8GWX0.
    SMRiB8GWX0. Positions 386-632.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini497 – 627131HDUniRule annotationAdd
    BLAST
    Domaini737 – 82185ACT 1UniRule annotationAdd
    BLAST
    Domaini848 – 92982ACT 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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF01842. ACT. 1 hit.
    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.

    B8GWX0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRRLRPTRL EHVVDGHALR ARLSAAALDS IGNEAEQRAR AIDILKQALF    50
    RGRMIAKERL ENGASGVETS RLLSGVTDEV ITALYDFTTV HVFRARNPTE 100
    GERLCLLAVG GYGRGTLAPF SDIDLLFLRP YKQTPHAESV IEYMLYALWD 150
    LGFKVGHASR TIEECVRLSK EDFTIRTSIL EARRLTGDER LAEDLKKRFR 200
    DEVMKATGAQ FVAAKLKERD DRQARAGASR YMVEPNVKEG KGGLRDLHTL 250
    MWIAEYLHPV DRPEDVFKME VFSIRETKAF IRAFDFLHAV RAHLHFTTGR 300
    PEERLTFDLQ PEIARRMGYG DRGDAPAVER FMRRYFLIAK EVGTLTRAFS 350
    AKLEAEHFKN EPKGISRFLP GARPKRKALD VEGFYEDGGR LNIEGQEIFE 400
    ADPVNLIRLF KIADERDLDL HPDAFTAVTR ALPLITSRVR RDPDACRAFL 450
    DLLARGKRSY RTLTLMNDAG VLGRFIPEFG RVVAQMQFNM YHSYTVDEHT 500
    LRAVGVIGDI AAGRLVDDHP LAVSIMPLIE DREALFLAML LHDTGKGGVG 550
    GQEKAGARSA RSACERLGVE RSKVELVAWL VENHLVMSDF AQKRDVSDPG 600
    TVAAFARIVE NPERLRLLLV ITVADIRAVG PGVWNGWKGQ LLRELYNATE 650
    AVFRGGRGSD AAANVQRHQE STAEAARAAL LETDPAAKGW VAAMENAYFS 700
    AFSQDDLFHH AELARRAAIQ GGAAAEGQVR PGSNAAEVVI AAKDRRGLFA 750
    DLALAISSLG GNVVGARVFT SRQGQALDVF YVQDVTGAPF GCENPRALRR 800
    LADALEAAGK GDALAVEPRR GSEQTRAAAF AIAPSVTIDN DASNDATVVE 850
    ASGRDRPGLL HALAKTLADS ALSIQSAHID GYGERAVDAF YVQTTEGGKV 900
    TDTRKLNALK ADLLAALEQN EASAPAARPG LRRARASVAR 940
    Length:940
    Mass (Da):103,396
    Last modified:March 3, 2009 - v1
    Checksum:i2F1985420353F8ED
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001340 Genomic DNA. Translation: ACL93480.1.
    RefSeqiWP_010917903.1. NC_011916.1.
    YP_002515388.1. NC_011916.1.

    Genome annotation databases

    EnsemblBacteriaiACL93480; ACL93480; CCNA_00013.
    GeneIDi7332895.
    KEGGiccs:CCNA_00013.
    PATRICi21304593. VBICauCre52860_0014.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001340 Genomic DNA. Translation: ACL93480.1 .
    RefSeqi WP_010917903.1. NC_011916.1.
    YP_002515388.1. NC_011916.1.

    3D structure databases

    ProteinModelPortali B8GWX0.
    SMRi B8GWX0. Positions 386-632.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 190650.CC_0013.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACL93480 ; ACL93480 ; CCNA_00013 .
    GeneIDi 7332895.
    KEGGi ccs:CCNA_00013.
    PATRICi 21304593. VBICauCre52860_0014.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CAULONA1000:CCNA_00013-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. 1 hit.
    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. "The genetic basis of laboratory adaptation in Caulobacter crescentus."
      Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., Walunas T.L., Crosson S.
      J. Bacteriol. 192:3678-3688(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NA1000 / CB15N.

    Entry informationi

    Entry nameiGLND_CAUCN
    AccessioniPrimary (citable) accession number: B8GWX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 44 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