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A4VJR9

- GLND_PSEU5

UniProt

A4VJR9 - GLND_PSEU5

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pseudomonas stutzeri (strain A1501)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (29 May 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 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

    BioCyciPSTU379731:GJER-1534-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:PST_1535
    OrganismiPseudomonas stutzeri (strain A1501)
    Taxonomic identifieri379731 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000000233: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000078809Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi379731.PST_1535.

    Structurei

    3D structure databases

    ProteinModelPortaliA4VJR9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini462 – 590129HDUniRule annotationAdd
    BLAST
    Domaini706 – 78984ACT 1UniRule annotationAdd
    BLAST
    Domaini816 – 89681ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 342342UridylyltransferaseAdd
    BLAST
    Regioni343 – 705363Uridylyl-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. 1 hit.
    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.

    A4VJR9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPQVDPELFD RSQFQAELAL KASPIAAYKK AIRQARQVLD ERFRAGRDIR    50
    RLIEDRAWFV DQILRSAWSR FDWDKGADIA LVAVGGYGRG ELHPYSDIDL 100
    LILLDENDQE IFREPIEGFL TLLWDIGLEV GQAVRSVAEC ADEARADLTV 150
    ITNLMESRTI AGPERLRQAM LQVTSTQQMW PSKEFFLAKR NEQRARHAKY 200
    NNTEYNLEPN VKGSPGGLRD IQTILWIARR EFGTLNLQAM VDQGFITEGE 250
    HSLLTAAQEF LWKVRYGLHM LAGRAEDRLL FDHQRSLAAL LGYEDSDAKL 300
    AIERFMQKYY RVVMSIAELS DLVGQHFAEV ILWEGESGPI VPLNSRFQVR 350
    DGYLEVSNPA IFKRTPFAIL ETFVLLAQHP DIQGVRSDTI RLLRDHRYLI 400
    DDTFRQDLRN TSLFIELFKC KEGIHRNLRR MNRYGILGRY LPEFGHIVGQ 450
    MQHDLFHIYT VDAHTLNVIK YLRKLTKPGV AEKYPLASKL VEKLPKPELI 500
    YIAGLYHDIA KGRGGDHSEL GAVDAEQFCR RHKLPAWDTR LVVWLVENHL 550
    VMSTTAQRKD LSDPQVINDF AQRVGDETHL DYLYVLTVAD INATNPTLWN 600
    SWRASLLRQL YTETKRALKR GLENPLGREE QIRQTQRAAL DDLVRHGTDP 650
    DDAEQLWAQL GDDYFLRHTA TDVAWHTDAI IEHPANGGPL VLIKETTQRE 700
    FEGGTQIFIY APDQHDFFAV TVAAMDQLNL NIHDARILTS SSQFTLDTYI 750
    VLEADGSPIG NNPERIEEIR SGLIAALRNP DDYLTIIQRR VPRQLKHFAF 800
    PPQVTIHNDT QRPQTILEII APDRPGLLAR VGQLFLDFDL SVQNAKIATL 850
    GERVEDVFFV TDADNQPLSD PQLCLRLQQA IIKELQQENE QQPSPSSIVI 900
    Length:900
    Mass (Da):102,974
    Last modified:May 29, 2007 - v1
    Checksum:i71172F92D9FFEF11
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000304 Genomic DNA. Translation: ABP79220.1.
    RefSeqiYP_001172062.1. NC_009434.1.

    Genome annotation databases

    EnsemblBacteriaiABP79220; ABP79220; PST_1535.
    GeneIDi5097620.
    KEGGipsa:PST_1535.
    PATRICi19963513. VBIPseStu31643_1536.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000304 Genomic DNA. Translation: ABP79220.1 .
    RefSeqi YP_001172062.1. NC_009434.1.

    3D structure databases

    ProteinModelPortali A4VJR9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 379731.PST_1535.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP79220 ; ABP79220 ; PST_1535 .
    GeneIDi 5097620.
    KEGGi psa:PST_1535.
    PATRICi 19963513. VBIPseStu31643_1536.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PSTU379731:GJER-1534-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. 1 hit.
    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 genome sequence of the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."
      Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y.
      , Elmerich C., Lin M., Jin Q.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: A1501.

    Entry informationi

    Entry nameiGLND_PSEU5
    AccessioniPrimary (citable) accession number: A4VJR9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 56 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