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Q6D8E5

- GLND_PECAS

UniProt

Q6D8E5 - GLND_PECAS

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      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 fixation 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 fixation Source: UniProtKB-HAMAP
    2. regulation of nitrogen utilization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Nitrogen fixation

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciPATR218491:GJNB-1059-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:ECA1029
    OrganismiPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
    Taxonomic identifieri218491 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
    ProteomesiUP000007966: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 904904Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192731Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi218491.ECA1029.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6D8E5.
    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.

    Q6D8E5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDKRFSPDN TPPDASSPDS PIDTIAAAQP PVSPLTYADD MLNCQALKQQ    50
    LELFQLWLGS EFRSGVSAEK LIDARTLFID RLLQRLWYCH GFENIAQTAL 100
    VAVGGYGRGE LHPLSDIDVL VLSQTELSDE HSQRVGQFIT LLWDLKLEVG 150
    HSVRTLEECL QEGRADISVA TNLIESRMIC GDVALFLTLQ KHVFSDEFWP 200
    SPTFFPAKIT 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 LFMNILRHPY AVSRALLPMH 450
    RHSVLWAYMP LWGNIVGQMQ FDLFHAYTVD EHTIRVLLKL ESFADEDTRP 500
    QHPLCVELYP RLPQPELLLL AALFHDIAKG RGGDHSELGA LDVLEFAALH 550
    GLNSREAQLV SWLVRCHLLM SVTAQRRDIQ DPTVIQQFAT EVQSETRLRY 600
    LVSLTVADIC ATNETLWNSW KQSLLRELYF ATEKQLRRGM QNTPDLRERV 650
    RHHRLQALAL LRMDNIDEEA LHHIWSRCRA DYFLRHSPNQ IAWHARHLLE 700
    HDTNKPLVLI SHQASRGGTE IFIWSPDRPY LFAAVAGELD RRNLSVHDAQ 750
    IFTSRDGMAM DTFIVLEPDG SPLAQDRHEM IRHALEQALT QRHYQHPRVR 800
    RTSPKLRHFS VPTEVNFLPT HTDRRSYMEL SALDQPGLLA RIGEIFSDLN 850
    LSLHGARIST IGERVEDLFI LADSDRRALK PELRLKLQER LTEALNPNDK 900
    VPLS 904
    Length:904
    Mass (Da):104,412
    Last modified:August 16, 2004 - v1
    Checksum:i1A6A4DEF5361ED32
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX950851 Genomic DNA. Translation: CAG73940.1.
    RefSeqiYP_049136.1. NC_004547.2.

    Genome annotation databases

    EnsemblBacteriaiCAG73940; CAG73940; ECA1029.
    GeneIDi2881763.
    KEGGieca:ECA1029.
    PATRICi20477274. VBIPecAtr54885_1037.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX950851 Genomic DNA. Translation: CAG73940.1 .
    RefSeqi YP_049136.1. NC_004547.2.

    3D structure databases

    ProteinModelPortali Q6D8E5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 218491.ECA1029.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG73940 ; CAG73940 ; ECA1029 .
    GeneIDi 2881763.
    KEGGi eca:ECA1029.
    PATRICi 20477274. VBIPecAtr54885_1037.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PATR218491:GJNB-1059-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SCRI 1043 / ATCC BAA-672.

    Entry informationi

    Entry nameiGLND_PECAS
    AccessioniPrimary (citable) accession number: Q6D8E5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 71 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