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Q3SWE0

- GLND_NITWN

UniProt

Q3SWE0 - GLND_NITWN

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      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

    BioCyciNWIN323098:GJEG-134-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:Nwi_0133
    OrganismiNitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
    Taxonomic identifieri323098 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
    ProteomesiUP000002531: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 925925Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231682Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi323098.Nwi_0133.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3SWE0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini500 – 59697HDUniRule annotationAdd
    BLAST
    Domaini739 – 82082ACT 1UniRule annotationAdd
    BLAST
    Domaini849 – 92577ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 382382UridylyltransferaseAdd
    BLAST
    Regioni383 – 738356Uridylyl-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.
    HOGENOMiHOG000261779.
    KOiK00990.
    OMAiLYCLWDM.
    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.

    Q3SWE0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLPTTKDAT AAGAGFDTVR IIGDIDALAE KHAGHEDVFR SAVSRLLKAE    50
    LAKVRDAAQA KLLRDRHGRH CAEWLCFVQD EIIRLSFSAA TRHLYHSPIP 100
    SDGERMAVVA TGGYGRGLMA PESDIDLLFI LPYKQTAWGE QVAEAILYCL 150
    WDMGLNVGHA TRSVNESIRQ ARRDMTVRTG ILEARFLTGD RALYDELISR 200
    FDTEVVQGTA AEFVAAKLAE REERHHRAGQ SRYLVEPNVK DGKGGLRDLH 250
    TLFWIAKYVY RVRESHELLR RNVFDVREYR TFRRCADFLW SVRCNLHFAT 300
    GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLT AKDVGDLTAI 350
    LCAKLEDQQA KPAPVLSRAM SKPPGAEVRR VPDSDDFIID NNRINLAAPD 400
    LFKRDPVNLI RLFRLAQKNN LAFHPDALRM VRRSRRLINA QLREDPESNR 450
    LFIEILTSND AETVLRRMNE TGVLGEFIRA FGKIVSMMQF NMYHHYTVDE 500
    HLIRCIGILQ DIERGDNDEV ALAGELMRTI NPEHRPVIYI ATLLHDVAKG 550
    RPEDHSIAGA RVARRLCPRL GFNAADTELV AWLIEQHLTM SKVAQSRDLS 600
    DRKTIENFAA VVQSVERMKL LTILTTADIR GVGPGVWNGW KAQLLRTLYY 650
    ETEPVLTGGF SEVNRAQRMA AAEAEFRAAF TEWSGHELNA YIARHYPAYW 700
    LKVDLEHKIR HARFLRASEQ SGRKLNINVG FDEARGVTEL TILAADHPWL 750
    LSIIAGACAS AGANIVDAQI YTTTDGQALD TIAISREYER DEDEGRRAAR 800
    IAEIIEQVLE GRLRLPDVMP SRAAGKRLRP FVVEPKVTIN NQWSDRHTMI 850
    EVSGLDRPGL LFQLTTAISK LNLNIASAHV ATFGERARDV FYVTDLLGAR 900
    ITAPTRQAAI KRALVHLLAS GNTAE 925
    Length:925
    Mass (Da):104,377
    Last modified:October 11, 2005 - v1
    Checksum:i9B4D8076280C0070
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000115 Genomic DNA. Translation: ABA03401.1.
    RefSeqiYP_316753.1. NC_007406.1.

    Genome annotation databases

    EnsemblBacteriaiABA03401; ABA03401; Nwi_0133.
    GeneIDi3676202.
    KEGGinwi:Nwi_0133.
    PATRICi22696587. VBINitWin102302_0149.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000115 Genomic DNA. Translation: ABA03401.1 .
    RefSeqi YP_316753.1. NC_007406.1.

    3D structure databases

    ProteinModelPortali Q3SWE0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 323098.Nwi_0133.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABA03401 ; ABA03401 ; Nwi_0133 .
    GeneIDi 3676202.
    KEGGi nwi:Nwi_0133.
    PATRICi 22696587. VBINitWin102302_0149.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261779.
    KOi K00990.
    OMAi LYCLWDM.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci NWIN323098:GJEG-134-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 chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
      Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
      Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Nb-255 / ATCC 25391.

    Entry informationi

    Entry nameiGLND_NITWN
    AccessioniPrimary (citable) accession number: Q3SWE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 62 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