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Q87MD6

- GLND_VIBPA

UniProt

Q87MD6 - GLND_VIBPA

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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

    BioCyciVPAR223926:GHK4-2377-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:VP2320
    OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
    Taxonomic identifieri223926 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000002493: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 874874Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192773Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi223926.VP2320.

    Structurei

    3D structure databases

    ProteinModelPortaliQ87MD6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini452 – 584133HDUniRule annotationAdd
    BLAST
    Domaini693 – 77785ACT 1UniRule annotationAdd
    BLAST
    Domaini800 – 87475ACT 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.

    Q87MD6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLQSPLTFS DEQINIGELK QELEKFSSTQ KQEFLNHHPV TSLVLARAEY    50
    MDLLLTRLWQ YFGFNDIYNI SLVAVGGYGR GELHPLSDID ILVLSNNKLP 100
    TALEAKISEF ITLLWDLKLE VGHAVRTVNE CAQIGRDDLT VATNLQEARL 150
    LCGSEDTFQA LKKVVLSDSF WPSETFYRAK IQEQRERHAR YHDTTYNLEP 200
    DIKSTPGGLR DIHTLSWVAR RHFGATSLLE MSRYGFLTDA EYRELVECQD 250
    FLWRVRFALH IELRRYDNRL TFAHQAQVAE NLGYVGEGNR GVEMMMKEFY 300
    RTLRRVAELN KMLLKLFDQA IINGGATENA EILDADFQRR GSLIEARKPA 350
    LFQARPETIL DMFLHIANDS TIEGVSPPTL RQLRTARRRL NKFLHTIPAA 400
    REKFLALCRH PNALHKAFSL MHRLGVMAAY LPQWSQIVGQ MQFDLFHAYT 450
    VDEHSIRLLK HINTFNNPDN HAKHPICCDI YPRMQKKELL IIAAIFHDIG 500
    KGRGGDHSVI GEGEAYDFCI EHGLSKPEAK LVGWLVRHHL LMSVTAQRRD 550
    IYDPDVITEF AKQVRDEESL EYLVCLTVAD ICATNPELWN AWKRTLLAEL 600
    FYSTQRALRR GLENPVDVRE RIRHNQQMAS ALLRKEGFSA RQIEVLWQRF 650
    KADYFLRHTH TQIAWHCAHL LRMDDPNKPL VLISKKATRG GTEVFVYTKD 700
    QPALFATVVA ELDRRNFNVH DAQIMTSKDG HVIDTFMVLD QHGEAIDESR 750
    HAAVIKHLTH VLEAGRPTKI KTRRTPNKLQ HFNVKTKVDF LPTKGKKHTL 800
    MEFVALDTPG LLAKVGRTFA DLNINLHGAK ITTIGERAED LFILTSEAGG 850
    RLSEEQQNEL RDKLIEKLSD AVTA 874
    Length:874
    Mass (Da):100,247
    Last modified:June 1, 2003 - v1
    Checksum:i1B849BC63393E97E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000031 Genomic DNA. Translation: BAC60583.1.
    RefSeqiNP_798699.1. NC_004603.1.

    Genome annotation databases

    EnsemblBacteriaiBAC60583; BAC60583; BAC60583.
    GeneIDi1189833.
    KEGGivpa:VP2320.
    PATRICi20142786. VBIVibPar50997_2222.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000031 Genomic DNA. Translation: BAC60583.1 .
    RefSeqi NP_798699.1. NC_004603.1.

    3D structure databases

    ProteinModelPortali Q87MD6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 223926.VP2320.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC60583 ; BAC60583 ; BAC60583 .
    GeneIDi 1189833.
    KEGGi vpa:VP2320.
    PATRICi 20142786. VBIVibPar50997_2222.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci VPAR223926:GHK4-2377-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 Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
      Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
      Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RIMD 2210633.

    Entry informationi

    Entry nameiGLND_VIBPA
    AccessioniPrimary (citable) accession number: Q87MD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 77 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