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A7MGS0

- GLND_CROS8

UniProt

A7MGS0 - GLND_CROS8

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (02 Oct 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

    BioCyciCSAK290339:GJ80-3166-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:ESA_03176
    OrganismiCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii)
    Taxonomic identifieri290339 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter
    ProteomesiUP000000260: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 892892Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022342Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi290339.ESA_03176.

    Structurei

    3D structure databases

    ProteinModelPortaliA7MGS0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini470 – 603134HDUniRule annotationAdd
    BLAST
    Domaini711 – 79080ACT 1UniRule annotationAdd
    BLAST
    Domaini818 – 89275ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 351351UridylyltransferaseAdd
    BLAST
    Regioni352 – 710359Uridylyl-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.

    A7MGS0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMSNTLPEQS VNTTLAPLPG QPDYPATWPA DALNCAQIKQ HLDAFQQWLG    50
    AAFDDGYTAE QLIEARTEFI DQLLQRLWIA AGFGDTPDTA LVAVGGYGRG 100
    ELHPLSDIDL LILSRKRLSE AQAQKVGELL TLLWDVKLEV GHSVRTLEEC 150
    LLEGLSDLTV ATNLIESRLL IGDVALFLEL QKHIFSDGFW PSEKFFAAKV 200
    EEQNERHQRY HGTSYNLEPD IKSSPGGLRD IHTLQWVARR HFGATSLREM 250
    VGFGFLTEAE RNELDECQHL LWRIRFALHL ELNRYDNRLL FDRQLSVAQR 300
    LRYEGEGNEP VEHMMKDFYR VTRRVGELNQ MLLQLFDEAI LALTTDEKPR 350
    VLDDDFQLRG TLIDLRDETL FIREPQAILR MFYMMVRNRD ITGIYSTTLR 400
    HLRHARRHLK QPLCYIPEAR SLFLAMLRHP GAVSRGLLPM HRHSVLWAYM 450
    PQWSHIVGQM QFDLFHAYTV DEHTIRVLLK LESFAKEETR AKHPLCVDLW 500
    PRLSHPELIL IAALFHDIAK GRGGDHSVLG AQDILKFAEL HGLNSRETQL 550
    VAWLVRHHLL MSVTAQRRDI QDPEVIKQFA EEVQTENRLR FLVCLTVADI 600
    CATNETLWNS WKQSLLRELY FATEKQLRRG MQSTPDMRER VRHHQLQALA 650
    LLRMENIDEE ALHHIWGRCR ANYFVRHSPN QLAWHARHLL RHDLSKPLIL 700
    LSPQATRGGT EIFIWSPDRP YLFAAVCAEL DRRNLSVHDA QIFTTRDDMA 750
    MDTFIVLEPD GSPLSPDRHE AIRHGLEQAI TQRTWQPPQP RRQPAKLRHF 800
    TVETEVNFLP THTDRKSFLE LIALDQPGLL ARVGQVFADL GISLHGARIS 850
    TIGERVEDLF IIATADRRGL NNLLQQEVRQ RLTEDLNPND KV 892
    Length:892
    Mass (Da):103,003
    Last modified:October 2, 2007 - v1
    Checksum:i99E2B1D75E7F6B4E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000783 Genomic DNA. Translation: ABU78398.1.
    RefSeqiWP_012125716.1. NC_009778.1.
    YP_001439234.1. NC_009778.1.

    Genome annotation databases

    EnsemblBacteriaiABU78398; ABU78398; ESA_03176.
    GeneIDi5549477.
    KEGGiesa:ESA_03176.
    PATRICi20398085. VBICroSak107175_2807.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000783 Genomic DNA. Translation: ABU78398.1 .
    RefSeqi WP_012125716.1. NC_009778.1.
    YP_001439234.1. NC_009778.1.

    3D structure databases

    ProteinModelPortali A7MGS0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 290339.ESA_03176.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABU78398 ; ABU78398 ; ESA_03176 .
    GeneIDi 5549477.
    KEGGi esa:ESA_03176.
    PATRICi 20398085. VBICroSak107175_2807.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CSAK290339:GJ80-3166-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. "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
      Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
      PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-894.

    Entry informationi

    Entry nameiGLND_CROS8
    AccessioniPrimary (citable) accession number: A7MGS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 51 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