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Q3SKP1

- GLND_THIDA

UniProt

Q3SKP1 - GLND_THIDA

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Thiobacillus denitrificans (strain ATCC 25259)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (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

    BioCyciTDEN292415:GHWG-804-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:Tbd_0783
    OrganismiThiobacillus denitrificans (strain ATCC 25259)
    Taxonomic identifieri292415 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus
    ProteomesiUP000008291: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 850850Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231695Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi292415.Tbd_0783.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3SKP1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini437 – 546110HDUniRule annotationAdd
    BLAST
    Domaini674 – 75582ACT 1UniRule annotationAdd
    BLAST
    Domaini783 – 85068ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 317317UridylyltransferaseAdd
    BLAST
    Regioni318 – 673356Uridylyl-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.
    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]
    PfamiPF08335. 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.

    Q3SKP1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSARPFADLR ERLKSGRASL AAAYREKPRA AHYLARHAAL VDALLAELST    50
    RLGLARGICL VAVGGYGRGE LFPGSDVDVM LLLPAEPLEA ERQALESWVQ 100
    ACWDVGLEIG HSVRTVDACL AEADADITVE TNLLEARRVW GATALFDDFG 150
    RRFRARFDAQ RFFDGKLAEQ HARHARFDDS AYKLEPNLKD SPGGLRDLHT 200
    IHWLAQACDI DAGWSGIARA GLLTEGEARR VAREERWLAK LRIHLHLLAG 250
    RREDRLAFDY QSELAACLGL APTAHRRAGE RLMQGYFRAA KLVQRANDIL 300
    IQSLRVRLFP VVAPPLPIDD DFQLRAGLLE ARDPDVFLRK PDALLRAFLV 350
    YARHPQLAGF EPTTLRAVWR ASARVDRAFR ATPAHRALFI ALLREPLGVT 400
    RALRAMHRYG LLGRYIPAFG RIVGQMQHDL FHVYTVDEHI LTVLRNLRRF 450
    TVAQLAHEFP LASRLIAAFD KPELLYLAAL FHDIAKGRGG DHSALGALDA 500
    RGFCRQHGLD KTDTDLVAWL VDMHLVMSRT SQKEDISDPK VIAAFAARVG 550
    DTRRLDALYL LTVADIRGTS PTVWNAWKGK LLEDLYHAAF ARLQGADLAI 600
    AGIAARREEA RVNLALYGLP RDAADALWRH LDKAYFARFD ARDMAWHARM 650
    LWRRDATAGA VVRARLSPAG EGIQVMVYAP DRPDIFVRIC AFFARIQYTV 700
    LEAKIHTTRN GYALDSFQVM DLAHRNIHYR DFLAFVEYEL ARDLDPARPL 750
    QAVQPGRLSR HQRHHPYPAA VHLEADRGGD GQVLSITCAD RGGLLFAIAE 800
    ELMRHEISVY AAKIDTLGER VEDTFLIRGE RLNAPPERAA LENELRGVLG 850
    Length:850
    Mass (Da):95,305
    Last modified:October 11, 2005 - v1
    Checksum:iAA673373E9F73EE8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000116 Genomic DNA. Translation: AAZ96736.1.
    RefSeqiYP_314541.1. NC_007404.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ96736; AAZ96736; Tbd_0783.
    GeneIDi3673977.
    KEGGitbd:Tbd_0783.
    PATRICi23967735. VBIThiDen82923_0782.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000116 Genomic DNA. Translation: AAZ96736.1 .
    RefSeqi YP_314541.1. NC_007404.1.

    3D structure databases

    ProteinModelPortali Q3SKP1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 292415.Tbd_0783.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ96736 ; AAZ96736 ; Tbd_0783 .
    GeneIDi 3673977.
    KEGGi tbd:Tbd_0783.
    PATRICi 23967735. VBIThiDen82923_0782.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci TDEN292415:GHWG-804-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 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. "The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
      Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
      J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25259.

    Entry informationi

    Entry nameiGLND_THIDA
    AccessioniPrimary (citable) accession number: Q3SKP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 64 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