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B5F8S8

- GLND_SALA4

UniProt

B5F8S8 - GLND_SALA4

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Salmonella agona (strain SL483)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (14 Oct 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

    BioCyciSENT454166:GHBA-248-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:SeAg_B0253
    OrganismiSalmonella agona (strain SL483)
    Taxonomic identifieri454166 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000008819: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 890890Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000114759Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi454166.SeAg_B0253.

    Structurei

    3D structure databases

    ProteinModelPortaliB5F8S8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini468 – 601134HDUniRule annotationAdd
    BLAST
    Domaini709 – 78476ACT 1UniRule annotationAdd
    BLAST
    Domaini816 – 89075ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 349349UridylyltransferaseAdd
    BLAST
    Regioni350 – 708359Uridylyl-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.
    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.

    B5F8S8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTLPEQHAN TALPTLPDQP QNPGVWPRAE LTVAGIKARI DIFQHWLGEA    50
    FDSGICAEQL IEARTEFIDQ LLQRLWIEAG FGQIADLALV AVGGYGRGEL 100
    HPLSDIDLLI LSRKKLPDEQ AQKVGELLTL LWDVKLDVGH SVRTLEECLL 150
    EGLSDLTVAT NLIETRLLIG DVALFLALQK HIFSEGFWPS DKFYAAKVEE 200
    QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF GATSLDEMVG 250
    FGFLTPAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN 300
    YSGEGNDPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPV 350
    DDEFQLRGTL IDLRDDTLFI REPQAILRMF YMMVRNSAIT GIYSTTLRHL 400
    RHARRHLSQP LCYIPEARTL FLSMLRHPGA VSRGLLPMHR HSVLWAYMPQ 450
    WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE SFAKEETRQR HPLCVDLWPR 500
    LPHPELILIA ALFHDIAKGR GGDHSVLGAQ DVLTFAELHG LNSRETQLVA 550
    WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTETRLRFL VCLTVADICA 600
    TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL 650
    RMDNIDEAAL HKIWTRCRAN YFVRHSPNQL AWHARHLLQH DLSQPLVLLS 700
    PQATRGGTEI FIWSPDRPYL FAAVCAELDR RNLSVHDAQI FTTRDGMAMD 750
    TFIVLEPDGN PLAADRHDVI RTGLEQTITQ RSWQPPQPRR QPAKLRHFTV 800
    ETEVNFLPTH TDRKSFMELI ALDQPGLLAR VGQIFADLGI SLHGARITTI 850
    GERVEDLFII ATADRRALNN VLQLEVQQRL TAALNPNDKG 890
    Length:890
    Mass (Da):102,222
    Last modified:October 14, 2008 - v1
    Checksum:i313D763DCCF77460
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001138 Genomic DNA. Translation: ACH49835.1.
    RefSeqiYP_002145219.1. NC_011149.1.

    Genome annotation databases

    EnsemblBacteriaiACH49835; ACH49835; SeAg_B0253.
    PATRICi18478870. VBISalEnt65316_0278.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001138 Genomic DNA. Translation: ACH49835.1 .
    RefSeqi YP_002145219.1. NC_011149.1.

    3D structure databases

    ProteinModelPortali B5F8S8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 454166.SeAg_B0253.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACH49835 ; ACH49835 ; SeAg_B0253 .
    PATRICi 18478870. VBISalEnt65316_0278.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SENT454166:GHBA-248-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. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
      Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
      J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SL483.

    Entry informationi

    Entry nameiGLND_SALA4
    AccessioniPrimary (citable) accession number: B5F8S8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 45 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