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A9R397

- GLND_YERPG

UniProt

A9R397 - GLND_YERPG

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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

    BioCyciYPES349746:GHPB-3448-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:YpAngola_A3437
    OrganismiYersinia pestis bv. Antiqua (strain Angola)
    Taxonomic identifieri349746 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000001204: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 893893Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000114770Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi349746.YpAngola_A3437.

    Structurei

    3D structure databases

    ProteinModelPortaliA9R397.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini470 – 603134HDUniRule annotationAdd
    BLAST
    Domaini711 – 79383ACT 1UniRule annotationAdd
    BLAST
    Domaini819 – 89375ACT 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.

    A9R397-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDNHTEHSL SLTLTPTISE QPALPSTYLD SDIHCPILKQ RLDAFQRWQA    50
    EAFNSGTSAE VLIAARSDYI DHLLQRLWTF YGFDKVPETA LVAVGGYGRG 100
    ELHPLSDIDV LVLSKQRLND EQAQRVGQLI TLLWDLKLEV GHSVRTLEEC 150
    LLEGLADLTI ATNMIESRLI CGDVALFLQM QKHIFSDSFW PSPQFFHAKV 200
    VEQQERHKRY HGTSYNLEPD IKSSPGGLRD IHTLLWVARR HFGATSLSEM 250
    VDFGFLTNAE RNELNESQSF LWRIRFALHL VLTRYDNRLL FDRQLSVAQL 300
    LRYEGEGNEP VEHMMKDFYR MTRRVSELNN MLLQLFDEAI LALDANEKPR 350
    PLDEEFQLRG DLIDLRDENL FVRQPEAIMR MFYLMVRNQD IKGIYSTTVR 400
    RLRHARRHLK APLCHIPEAR KLFMAILRHP GAVSRALLPM HRHSVLWAYM 450
    PQWGSIVGQM QFDLFHAYTV DEHTIRVLLK IESFADEDTR PRHPLCVELY 500
    PRLPQPELLL LAALFHDIAK GRGGDHSILG AHDAVEFAEQ HGLNSRESQL 550
    VAWLVRCHLL MSVTAQRRDI QDPAVIQQFS AEVQSETRLR YLVSLTVADI 600
    CATNENLWNS WKQSLLRELY FATEKQLRRG MQNSPDLRER VRHHRLQALA 650
    LLRMDNIDEE ALHRIWSRCR ADYFLRHSPN QLAWHARHLL EHDSTKPLVL 700
    VSRQATRGGT EIFIWSPDRP SLFAAVVGEL DRRNLSVHDA QIFTNRDGMA 750
    MDTFIVLEPD GSPLAQDRHP IISHALQQAI NRSDYQHPPR VRRLSPKLRH 800
    FSVPTEANFL PTHNERRTYL ELIALDQPGL LARVGKIFAD LGLSLHSARI 850
    TTIGERVEDL FVLADKDRRA LSLETRRELA QRLADTLNPN DKL 893
    Length:893
    Mass (Da):103,158
    Last modified:February 5, 2008 - v1
    Checksum:iAE09A7808DB3D611
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX88111.1.
    RefSeqiYP_001607773.1. NC_010159.1.

    Genome annotation databases

    EnsemblBacteriaiABX88111; ABX88111; YpAngola_A3437.
    GeneIDi5801914.
    KEGGiypg:YpAngola_A3437.
    PATRICi18576521. VBIYerPes97331_4015.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX88111.1 .
    RefSeqi YP_001607773.1. NC_010159.1.

    3D structure databases

    ProteinModelPortali A9R397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349746.YpAngola_A3437.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX88111 ; ABX88111 ; YpAngola_A3437 .
    GeneIDi 5801914.
    KEGGi ypg:YpAngola_A3437.
    PATRICi 18576521. VBIYerPes97331_4015.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci YPES349746:GHPB-3448-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 the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
      Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
      J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Angola.

    Entry informationi

    Entry nameiGLND_YERPG
    AccessioniPrimary (citable) accession number: A9R397
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 52 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