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Q31G41

- GLND_THICR

UniProt

Q31G41 - GLND_THICR

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Thiomicrospira crunogena (strain XCL-2)
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 (06 Dec 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

    BioCyciTCRU317025:GHE8-1320-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:Tcr_1287
    OrganismiThiomicrospira crunogena (strain XCL-2)
    Taxonomic identifieri317025 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira
    ProteomesiUP000002713: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 888888Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231696Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi317025.Tcr_1287.

    Structurei

    3D structure databases

    ProteinModelPortaliQ31G41.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini469 – 600132HDUniRule annotationAdd
    BLAST
    Domaini710 – 78778ACT 1UniRule annotationAdd
    BLAST
    Domaini817 – 88872ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 348348UridylyltransferaseAdd
    BLAST
    Regioni349 – 709361Uridylyl-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.

    Q31G41-1 [UniParc]FASTAAdd to Basket

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    MATTTDKQVS PTSPSFVYNL DHEDRNTSLK SGRAVLTDFN EQQFVKFDKG    50
    CSIETLLKER TSFIDQLLKK IWEHFFSKDE CEQLTLVAVG GYGRGELQPY 100
    SDIDLLILGE NFIELQPKIV EFITYLWDIG FEVGHAVRNL EDCIEAGRED 150
    VTTATNLLEA RWLAGNYEQF LSLQNLFNLK SFWPSHEFFQ AKLEEQEKRH 200
    KRYNDTLYQL EPNIKESPGG LRDIQTILWV AKRHFGASSL QELMQHNFIS 250
    LQEYKEIQAA YLYLNRIRFA LHRLKKRHED RLLFDHQQQL AELLNHDDRP 300
    EHNDSIKAVE AFMKPYYQNA HIVARLNEIL LQHFKEEIYH FAEDKIEPIN 350
    PRFRIINNYL DVVKENLFAK NPTALLEIFI IIENYQHLIQ GIRSRTIRLI 400
    RNHLHLIDDQ FRSDPINKAL FIEIFRQPKG VNAAVKRMYA YGILGAYLPS 450
    FKKITGLMQF NIFHAYTVDE HTILVIRNLR RFFIKQHAYE FPTAHQIATQ 500
    LCKPEILLLA GLFHDIAKGR NGAHEKLGAV DAKAFSQKHN LNKNDTDLLS 550
    WLVLRHLDFS YVAQKKDLSD PEIIQQFAEK VGTQQRLDYL YLLTLADVRS 600
    TSDEVWNDWK NQLFLQLYHN TTQALDSSSS QPRDRVKQAI FNKEKASELL 650
    KKRGLIPMHF QGFWQAFEQT DFFNRQSAAE IARITRVLFE EDHEAINIHL 700
    QPTTSRGATE LIIYMHDRDY LFAQFTQIID KLDLNIVEAK IYSGEDDMTL 750
    VIIYLLNRES TSITDPMILT EIEETLKHQL FLKDDTMPPT QPEPRRIRVF 800
    EMPTHIQFQE INEELTELSI STKDIPGLLA KIGQAFKSCK IRVHDAKINT 850
    VGEKAEDTFM ISSTTNESIH TRHSQEELKQ ALLNNIEQ 888
    Length:888
    Mass (Da):103,724
    Last modified:December 6, 2005 - v1
    Checksum:i842AEC6110A9F414
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000109 Genomic DNA. Translation: ABB41882.1.
    RefSeqiYP_391556.1. NC_007520.2.

    Genome annotation databases

    EnsemblBacteriaiABB41882; ABB41882; Tcr_1287.
    GeneIDi3761676.
    KEGGitcx:Tcr_1287.
    PATRICi23974592. VBIThiCru83387_1340.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000109 Genomic DNA. Translation: ABB41882.1 .
    RefSeqi YP_391556.1. NC_007520.2.

    3D structure databases

    ProteinModelPortali Q31G41.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 317025.Tcr_1287.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB41882 ; ABB41882 ; Tcr_1287 .
    GeneIDi 3761676.
    KEGGi tcx:Tcr_1287.
    PATRICi 23974592. VBIThiCru83387_1340.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci TCRU317025:GHE8-1320-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: XCL-2.

    Entry informationi

    Entry nameiGLND_THICR
    AccessioniPrimary (citable) accession number: Q31G41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: December 6, 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