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Q5QXT0

- GLND_IDILO

UniProt

Q5QXT0 - GLND_IDILO

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (04 Jan 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

    BioCyciILOI283942:GI0U-847-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:IL0847
    OrganismiIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
    Taxonomic identifieri283942 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina
    ProteomesiUP000001171: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 879879Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192738Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi283942.IL0847.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5QXT0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini478 – 590113HDUniRule annotationAdd
    BLAST
    Domaini701 – 78282ACT 1UniRule annotationAdd
    BLAST
    Domaini809 – 87971ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 340340UridylyltransferaseAdd
    BLAST
    Regioni341 – 700360Uridylyl-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.

    Q5QXT0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANVQEDKDF HGRWPDRTLQ PCLKDYKALL ESYQNWSAAR FVTADIDELV    50
    HHRATFFDQL ISQLWQQFQL EDEPASILAV GGYGRETLHP GSDIDLLILV 100
    GPENAEAEAK LSEKLGQFVT FLWDLHLDIG HSVRTIEDCF AQSENDITIA 150
    TNLIESRYLS GAESLYNEFH QQLLNDFPWS SRDFYQAKLD EQKQRHQQYH 200
    STSYNLEPNI KSSPGGLRDI QTVGWIAKRH FRTHSDENLV EYGYMTADEF 250
    VELRDCMNWL WRIRFALHLE AGKREDRLLF DFQPGVAVRL GYGNDGKASV 300
    ETMMKDYFKV VLRVSELNQM LLQFFHQAIL GTQDLQHAEH ISDDFAVANK 350
    LLTARHDNVF DNHCNIIRAF VCIAEHPQIQ GIHSNTIRLL RNARAQLSEP 400
    LSHDPECRDL FNQLIQHPRG CGLSFALMHH HSVLASYLSQ WQQIVGQMQF 450
    DLFHAYTVDE HTFRLVRNLY RFSDEDYQDQ FPLCEKLVAQ MDRRYCLYLA 500
    GIFHDIAKGR GGDHSELGEM DARNFCHQHG YSEEDAELVA WLVRHHLTMS 550
    VTAQKRDIHD PEVIQDFANQ VSTPERLDYL YCLTVADIRA TNQSLWNNWK 600
    ATLLEELYNA TSYLLQQDSN KPTLDIRQKI NENKASAMAL LLSAGFEKAE 650
    ILALWGRFTA DYFFRHTAEQ ISWHSQHILN LPSEQLPLIL IGDENNYGTT 700
    ELFIYHHEEG HLFASVAGVL DSQQLNILDA QILATRDGFV MDTFVVLQRD 750
    GKPLTEPHRI EEVKQQLLDV LHKRIPVPST KRPLSRRMKN FSVATEVTFI 800
    PSKHHGRTTF ELVTLDRPGL IAKLAAILQQ QNVILLAAKI TTIGEQAEDL 850
    FIVTTEQQTA LSDKQKKTLK AKIIKDLEF 879
    Length:879
    Mass (Da):101,332
    Last modified:January 4, 2005 - v1
    Checksum:i7DFEC2D5EA90098B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017340 Genomic DNA. Translation: AAV81687.1.
    RefSeqiWP_011234098.1. NC_006512.1.
    YP_155236.1. NC_006512.1.

    Genome annotation databases

    EnsemblBacteriaiAAV81687; AAV81687; IL0847.
    GeneIDi3173614.
    KEGGiilo:IL0847.
    PATRICi22139727. VBIIdiLoi21852_0849.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017340 Genomic DNA. Translation: AAV81687.1 .
    RefSeqi WP_011234098.1. NC_006512.1.
    YP_155236.1. NC_006512.1.

    3D structure databases

    ProteinModelPortali Q5QXT0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 283942.IL0847.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV81687 ; AAV81687 ; IL0847 .
    GeneIDi 3173614.
    KEGGi ilo:IL0847.
    PATRICi 22139727. VBIIdiLoi21852_0849.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci ILOI283942:GI0U-847-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: ATCC BAA-735 / DSM 15497 / L2-TR.

    Entry informationi

    Entry nameiGLND_IDILO
    AccessioniPrimary (citable) accession number: Q5QXT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 72 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