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)

Q2GAJ4

- GLND_NOVAD

UniProt

Q2GAJ4 - GLND_NOVAD

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (21 Mar 2006)
      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: 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

    BioCyciNARO279238:GHBU-690-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:Saro_0682
    OrganismiNovosphingobium aromaticivorans (strain DSM 12444 / F199)
    Taxonomic identifieri279238 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium
    ProteomesiUP000009134: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 912912Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000078807Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi279238.Saro_0682.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2GAJ4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini486 – 591106HDUniRule annotationAdd
    BLAST
    Domaini723 – 80280ACT 1UniRule annotationAdd
    BLAST
    Domaini834 – 91279ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 369369UridylyltransferaseAdd
    BLAST
    Regioni370 – 722353Uridylyl-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.
    HOGENOMiHOG000261779.
    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.

    Q2GAJ4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPRIANQRA IVDRRALADA VSAAFAEQGD RSRPAVVELL RGALDSGRAE    50
    LARRLEARPS AGTECAHGQA FLVDQLVRVI HDHVVGKVYR ASNRSTGERI 100
    AIIAVGGYGR GEMAPHSDVD IAFVTPIKPT SWCEQVIEAI LYFLWDLGLK 150
    VGHSSRSLDE VVRMAKSDLT IRTALLEGRY VWGDRDLFDA ASARFWNEVV 200
    NGTEKQFVAE KLQERNERHK RLGDSRYVVE PNVKEGKGGL RDLHTLYWIG 250
    KYIHKVRDAS ELVDVGLLTA EEYRAFRRAE NFFWAVRCHL HAITRRAEDR 300
    LTFDLQREVA MRMNFADRPG KSAVERFMQY FFLQAKQVGS LTGVFLAQLD 350
    GQFARQKRSF FASLRSRRKK VGPFFIEGGK LGVPAEDTFQ QDPVRLVELF 400
    AVAASEKVEI HPEAMRLARR DAGLIDAAVR KDQRANALFL DVLTSRNDPE 450
    TVLRWMNEAG VFGRFVPDFG RVVAQMQFDM YHHYTVDEHT IRAIGLLASI 500
    EKGEAKADHP LASEVVGKVA SRRVLYVATL LHDIAKGRRG DHSVLGAEVA 550
    MKLCPRLGLS AAETELVAWL VRWHLLMSAT AFKRDLADYK TIADFVNTVQ 600
    SQERLRLLLL LTIVDIRAVG PGVWNSWKRQ LLGDLFVSAE EVLRLGHKQH 650
    GRAERIIAKK KAVGAILKER DNLIGTVGRQ LGDAYWIAEP EDIIALNLQQ 700
    MDQALGELLS VEAHWYPARG ATLVTVLAAD HPGLFYRIAG GIHLAGGNII 750
    DARIHTARNG TAVDNFLVQD PLGRPLNEAS QIERLKNAIA DALANRVKLV 800
    PQLAARPLAR PRADAFDVRP IVIFDNKASN RFTVIEVGAR DRPALLNRLA 850
    RALFEARLIV HSAHIATYGE RAVDTFYVTD VLGEKVDSEA RMKAVEKRLL 900
    EAAEDRKVKD AA 912
    Length:912
    Mass (Da):101,972
    Last modified:March 21, 2006 - v1
    Checksum:iE81AD196FA1A216A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000248 Genomic DNA. Translation: ABD25129.1.
    RefSeqiWP_011444343.1. NC_007794.1.
    YP_495963.1. NC_007794.1.

    Genome annotation databases

    EnsemblBacteriaiABD25129; ABD25129; Saro_0682.
    GeneIDi3918107.
    KEGGinar:Saro_0682.
    PATRICi22783982. VBINovAro50627_0701.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000248 Genomic DNA. Translation: ABD25129.1 .
    RefSeqi WP_011444343.1. NC_007794.1.
    YP_495963.1. NC_007794.1.

    3D structure databases

    ProteinModelPortali Q2GAJ4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 279238.Saro_0682.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABD25129 ; ABD25129 ; Saro_0682 .
    GeneIDi 3918107.
    KEGGi nar:Saro_0682.
    PATRICi 22783982. VBINovAro50627_0701.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261779.
    KOi K00990.
    OMAi HHLLMSV.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci NARO279238:GHBU-690-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: DSM 12444 / F199.

    Entry informationi

    Entry nameiGLND_NOVAD
    AccessioniPrimary (citable) accession number: Q2GAJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 69 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