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B4RLK3

- GLND_NEIG2

UniProt

B4RLK3 - GLND_NEIG2

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Neisseria gonorrhoeae (strain NCCP11945)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (23 Sep 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

    Enzyme and pathway databases

    BioCyciNGON521006:GJ73-1037-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:NGK_1013
    OrganismiNeisseria gonorrhoeae (strain NCCP11945)
    Taxonomic identifieri521006 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000002564: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000114756Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi521006.NGK_1013.

    Structurei

    3D structure databases

    ProteinModelPortaliB4RLK3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini437 – 539103HDUniRule annotationAdd
    BLAST
    Domaini673 – 75785ACT 1UniRule annotationAdd
    BLAST
    Domaini785 – 85268ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 318318UridylyltransferaseAdd
    BLAST
    Regioni319 – 672354Uridylyl-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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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.

    B4RLK3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPENLSSALE TFKQQRNAAE AHYLKANRVS VFFREYTAAV ETLLAALWAE    50
    HFQNSALCLM AVGGFGRGEP YPCSDVDLAV VSPAPLSDGI QEQIARFIQT 100
    LWDCKLMPSV KSGSVDELCE SVRDDITGDT AFLEARFLFG NRQTADELAE 150
    KMNVQRNVAA FIEAKLVEME HRHAKSQGSG AVLEPNIKSC PGGLRDIHTL 200
    LWIAKAQGLA ANLPDLLKQR ILTRAEAGML SHGYRRLAHI RIRLHLNAKR 250
    AEDRLLFDLQ PQVAESMGYQ DENRRRQSEE LMRVFYRAVK TVKQLGGILT 300
    PMLRSRVSST PMRVTLRIDD DYIQVNNQIA ARHTDIFFRR PEHIFKIVEI 350
    MQQRNDITAL EPQTLRAWWG ATRKINRSFY QNSENRRRFA GFFRSGNGLT 400
    QTLRFLNLYG VLGRYLPAWE KIVGLLQHDL FHIYPVDDHI LAVVRNVRRL 450
    ALDMHSHELP YASALMQSFE KQDILYLAAF FHDIAKGRGG DHAVQGIADA 500
    RQFAADHFLT EEESDLLAWL VENHLLMSAV AQKEDIQDPG VLDAFCKRVQ 550
    THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RCLAGNDGNP 600
    HALFGRRRQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA 650
    NLVHDFEPPI VRSRILPQSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL 700
    AARAFITEHD YILDTFIVQI PSQHAPEDYP DIQSALEAEL NSFIHGHTVA 750
    ETQSCNRRIS RRSRYMPIAP SITITPEEDY PDRYSVEITA VNRPFLLADM 800
    AEVFFAHNVS LRYAKISTLD ERVEDSFTVF SPDLKNPKIQ SSLKQALLEQ 850
    LA 852
    Length:852
    Mass (Da):96,996
    Last modified:September 23, 2008 - v1
    Checksum:i4B3EC476F18EA2DE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001050 Genomic DNA. Translation: ACF29690.1.
    RefSeqiYP_002001638.1. NC_011035.1.

    Genome annotation databases

    EnsemblBacteriaiACF29690; ACF29690; NGK_1013.
    GeneIDi6447692.
    KEGGingk:NGK_1013.
    PATRICi20340474. VBINeiGon87511_1102.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001050 Genomic DNA. Translation: ACF29690.1 .
    RefSeqi YP_002001638.1. NC_011035.1.

    3D structure databases

    ProteinModelPortali B4RLK3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 521006.NGK_1013.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACF29690 ; ACF29690 ; NGK_1013 .
    GeneIDi 6447692.
    KEGGi ngk:NGK_1013.
    PATRICi 20340474. VBINeiGon87511_1102.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci NGON521006:GJ73-1037-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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view ]
    Pfami PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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 genome sequence of Neisseria gonorrhoeae NCCP11945."
      Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.
      J. Bacteriol. 190:6035-6036(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCCP11945.

    Entry informationi

    Entry nameiGLND_NEIG2
    AccessioniPrimary (citable) accession number: B4RLK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 43 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