Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9KPV0

- GLND_VIBCH

UniProt

Q9KPV0 - GLND_VIBCH

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: TIGR
    2. amino acid binding Source: InterPro
    3. metal ion binding Source: InterPro
    4. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. glutamine biosynthetic process Source: TIGR
    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:VC_2262
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000584: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 876876Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192771Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243277.VC2262.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9KPV0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini451 – 584134HDUniRule annotationAdd
    BLAST
    Domaini693 – 77785ACT 1UniRule annotationAdd
    BLAST
    Domaini800 – 87677ACT 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.
    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.

    Q9KPV0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPYQSPITFQ EPQLTVESLK QQLESFTEYQ KQEFFDHHPV TDLVLGRSEY    50
    MDLLLHRLWQ FFGFDELVEV SLVAVGGYGR GELHPLSDID LLVLSQQPLS 100
    EQVANKISQF LTLLWDLKLE IGHAVRTVEQ CAEIGKADLT VATNLQEARL 150
    LCGCEETFHR LKMVIHSESF WPSEIFYQAK VREQKERHAR YHDTTYNLEP 200
    DIKSTPGGLR DIHTLSWVAR RHFGATSLYE MSRFGFLTDA EYRELVECQD 250
    FLWRVRFALH IELKRYDNRL TFAHQVQVAR HLGYFGEGNR GIEMMMKEFF 300
    RTLRRVAELN KMLLKIFDKA ILNNGEEAEA VIIDDDFQRR GNMIEARKPA 350
    LFQARPETIL DMFLHMASDS TIESVAPATM RQLRTARRRL NKFLHTLPAA 400
    REKFIELVRH PNALHKAFSQ MHKLGVLAAY LPQWNQIVGQ MQFDLFHVYT 450
    VDEHSIRLLK HIHLFSDANN HDRHPICCEI YPKIQKKELL ILAAIFHDIG 500
    KGRGGDHSEI GADEAFDFCI EHGLSKPEAK LVAWLVKNHL LMSVTAQRRD 550
    IYDPDVIIEF AKKVRDEERL EYLVCLTVAD ICATNPELWN SWKRTLLAEL 600
    FYSTQRALRR GLENPVDVRE RIRHNQQMAS ALLRKEGFSS REIEVLWQRF 650
    KADYFLRHTH KQIAWHCTHL LRHEDSSKPL VLLSKKATRG GTEVFIYTKD 700
    QAALFATVVA ELDRRNLNVH DAQIMASKDG YVLDTFMVLD QNGQAIEEDR 750
    HQALIRHLVH VLEDGRPTTQ KARRIPRNLQ HFKVKTQVDF LPTKSKKRTL 800
    MEFVALDTPG LLATVGATFA ELNLDLHAAK ITTIGERAED LFILTNAQGT 850
    RLNEEEEQHL REKLIEHVAE LAPSAQ 876
    Length:876
    Mass (Da):101,542
    Last modified:July 5, 2004 - v2
    Checksum:iD7A48AB39C755C32
    GO

    Sequence cautioni

    The sequence AAF95406.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF95406.1. Different initiation.
    PIRiE82097.
    RefSeqiNP_231893.1. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF95406; AAF95406; VC_2262.
    GeneIDi2613184.
    KEGGivch:VC2262.
    PATRICi20083567. VBIVibCho83274_2158.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF95406.1 . Different initiation.
    PIRi E82097.
    RefSeqi NP_231893.1. NC_002505.1.

    3D structure databases

    ProteinModelPortali Q9KPV0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243277.VC2262.

    Protocols and materials databases

    DNASUi 2613184.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF95406 ; AAF95406 ; VC_2262 .
    GeneIDi 2613184.
    KEGGi vch:VC2262.
    PATRICi 20083567. VBIVibCho83274_2158.

    Phylogenomic databases

    eggNOGi COG2844.
    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. 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 39315 / El Tor Inaba N16961.

    Entry informationi

    Entry nameiGLND_VIBCH
    AccessioniPrimary (citable) accession number: Q9KPV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 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