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B5F9X8

- GLND_VIBFM

UniProt

B5F9X8 - GLND_VIBFM

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Vibrio fischeri (strain MJ11)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (14 Oct 2008)
      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

    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:VFMJ11_2098
    OrganismiVibrio fischeri (strain MJ11)
    Taxonomic identifieri388396 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
    ProteomesiUP000001857: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 873873Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000114768Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi388396.VFMJ11_2098.

    Structurei

    3D structure databases

    ProteinModelPortaliB5F9X8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini451 – 584134HDUniRule annotationAdd
    BLAST
    Domaini693 – 77785ACT 1UniRule annotationAdd
    BLAST
    Domaini800 – 87374ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 332332UridylyltransferaseAdd
    BLAST
    Regioni333 – 692360Uridylyl-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. 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.

    B5F9X8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKYLSPLSLS DTQLNITELK QQLTLFSQYQ INAFHQHKAV SDLVFERSHY    50
    FDQLLSRLWQ FFKFDDIANT SLIAVGGYGR SELHPLSDID ILILTENNTN 100
    DTFCQKVGEL VTLLWDLKLE IGHSVRSIAE CIEIGQNDLT VATNLQEARY 150
    ICGNKELSHQ LKLKIHSDSF WPSESFYQAK IDEQKKRHSR YHDTTYNLEP 200
    DIKSSPGGLR DIHTLSWIAR RHFGATSLLE MSQAGFLTDA EYRELLECQE 250
    FLWRVRFALH IELKRYDNRL TFGHQASVAE HLGFIGEGNR GVERMMKEFY 300
    RTLRRVAELN SMLLKIFDQA ILHQGEQDDA IIIDDDFQRR GRLIEARKPA 350
    LFQARPDTIL DMFLLMANDS TIDGVAPPTM RQLRTARRRL NRFLCEIPEA 400
    KEKFLQLTQH PNALNNAFSS MHKLGVLSAY LPQWSHIVGQ MQFDLFHAYT 450
    VDEHSIRLLK HINKFSDTTN RDKHPICCEI FPKIMKKELL IIAAIFHDIA 500
    KGRGGDHSEL GAVDAYDFCI SHGLSKPEAN LVSWLVKSHL LMSVTAQRRD 550
    IYDPDVITEF AKQVRDEERL DYLVCLTVAD ICATNPDLWN SWKRSLIADL 600
    YNATQRALRR GLENPPDLRD RIRHNQQMAS AQLRSEGFTQ WEVDALWRRF 650
    KADYFLRHTH KQIAWHASHL LRHQDKEKSL ILISKNASRG GTEIFVYSKD 700
    QPHLFATVAA ELDRRSITIY DAQVMSSKDG YALDTFMVLD QNDDPIDEER 750
    QQRLIDQLYD VKLNDQATHI KTRRPPRQLQ HFNVKTRMEF LPTKTGKRTL 800
    MEFVALDTPG LLATVGATFA QLGINLHAAK ITTIGERAED LFILTSDVGG 850
    RLDDDKQAEL EIALVKNVAR LSS 873
    Length:873
    Mass (Da):100,653
    Last modified:October 14, 2008 - v1
    Checksum:iBD26292DA8B5F8CD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001139 Genomic DNA. Translation: ACH66318.1.
    RefSeqiWP_012533646.1. NC_011184.1.
    YP_002156792.1. NC_011184.1.

    Genome annotation databases

    EnsemblBacteriaiACH66318; ACH66318; VFMJ11_2098.
    GeneIDi6806687.
    KEGGivfm:VFMJ11_2098.
    PATRICi20122660. VBIVibFis37164_2020.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001139 Genomic DNA. Translation: ACH66318.1 .
    RefSeqi WP_012533646.1. NC_011184.1.
    YP_002156792.1. NC_011184.1.

    3D structure databases

    ProteinModelPortali B5F9X8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 388396.VFMJ11_2098.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACH66318 ; ACH66318 ; VFMJ11_2098 .
    GeneIDi 6806687.
    KEGGi vfm:VFMJ11_2098.
    PATRICi 20122660. VBIVibFis37164_2020.

    Phylogenomic databases

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

    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. "Complete sequence of Vibrio fischeri strain MJ11."
      Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MJ11.

    Entry informationi

    Entry nameiGLND_VIBFM
    AccessioniPrimary (citable) accession number: B5F9X8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 46 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3