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C6DAI1

- GLND_PECCP

UniProt

C6DAI1 - GLND_PECCP

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (01 Sep 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

    BioCyciPCAR561230:GKCK-969-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:PC1_0939
    OrganismiPectobacterium carotovorum subsp. carotovorum (strain PC1)
    Taxonomic identifieri561230 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
    ProteomesiUP000002736: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 904904Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000204799Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi561230.PC1_0939.

    Structurei

    3D structure databases

    ProteinModelPortaliC6DAI1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini479 – 612134HDUniRule annotationAdd
    BLAST
    Domaini720 – 80182ACT 1UniRule annotationAdd
    BLAST
    Domaini827 – 90478ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 360360UridylyltransferaseAdd
    BLAST
    Regioni361 – 719359Uridylyl-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. 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.

    C6DAI1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDNRFSPDS TPPDASSPDS PVDTIASTQL PASPLTYADD MLNCQTLKQQ    50
    LELFQLWLGS EFRSGVSAEK LIDARTLFID RLLQRLWYFY GFENIAQTSL 100
    VAVGGYGRGE LHPLSDIDVL VLSQTALSEE HSQRVGQFIT LLWDLKLEVG 150
    HSVRTLEECL QEGRADISVA TNLIESRMIC GDVALFLTLQ KHVFSDEFWP 200
    SSAFFPAKIA EQQERHQRYH STSYNLEPDI KSSPGGLRDI HTLLWVARRH 250
    FGATSLNEMV GFGFLTEAER KELNECQSFL WRIRFALHLI LPRYDNRLLF 300
    DRQLNVAQLL QYQGEGNTPV ERMMKDFYRM TRRVSELNQM LLQLFDEAIL 350
    ALDASEKPRP IDDEFQLRGN LVDLRDENLF IKKPEAIMRM FYLMVRNRDI 400
    SGIYSTTLRQ LRHARRHLAS PLCTIPEARQ LFMNILRHPH AVSRALLPMH 450
    RHSVLWAYMP LWGNIVGQMQ FDLFHAYTVD EHTIRVLLKL ESFADEETRP 500
    QHPLCVELYP RLPQPELLLL AALFHDIAKG RGGDHSELGA QDVLEFAALH 550
    GLNSREAQLV SWLVRCHLLM SVTAQRRDIQ DPTVIQQFAT EVQSETRLRY 600
    LVSLTVADIC ATNETLWNSW KQSLLRELYF ATEKQLRRGM QNTPDLRERV 650
    RHHRLQALAL LRMDNIDEEA LHHIWSRCRA DYFLRHSPNQ LAWHARHLLE 700
    HDVNKPLVLI SHQASRGGTE IFIWSPDRPY LFAAVAGELD RRNLSVHDAQ 750
    IFTSRDGMAM DTFIVLEPDG SPLAQDRHEM IRHALEQALT QRHYQHPRVR 800
    RPSPKLRHFS VPTEVNFLPT HTDRRSYMEL SALDQPGLLA RIGEIFADLN 850
    LSLHGARIST IGERVEDLFI LADSDRRALK PELRLKLQER LTEALNPNDK 900
    VPLS 904
    Length:904
    Mass (Da):104,374
    Last modified:September 1, 2009 - v1
    Checksum:i8B64081DE776F27A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001657 Genomic DNA. Translation: ACT11989.1.
    RefSeqiWP_012773628.1. NC_012917.1.
    YP_003016525.1. NC_012917.1.

    Genome annotation databases

    EnsemblBacteriaiACT11989; ACT11989; PC1_0939.
    GeneIDi8131868.
    KEGGipct:PC1_0939.
    PATRICi20486468. VBIPecCar70489_0935.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001657 Genomic DNA. Translation: ACT11989.1 .
    RefSeqi WP_012773628.1. NC_012917.1.
    YP_003016525.1. NC_012917.1.

    3D structure databases

    ProteinModelPortali C6DAI1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 561230.PC1_0939.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACT11989 ; ACT11989 ; PC1_0939 .
    GeneIDi 8131868.
    KEGGi pct:PC1_0939.
    PATRICi 20486468. VBIPecCar70489_0935.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PCAR561230:GKCK-969-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. 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. "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.
      , Balakrishnan V., Glasner J., Perna N.T.
      Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PC1.

    Entry informationi

    Entry nameiGLND_PECCP
    AccessioniPrimary (citable) accession number: C6DAI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 42 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