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Q8RQD1

- GLND_AZOBR

UniProt

Q8RQD1 - GLND_AZOBR

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Azospirillum brasilense
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnZ, 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 fixation and metabolism.1 Publication

    Catalytic activityi

    UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].1 PublicationUniRule annotation
    Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].1 PublicationUniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Enzyme regulationi

    Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity. Uridylylation process is dependent on ATP and 2-oxoglutarate, which are effector molecules that likely bind to PII proteins and control their activity.1 PublicationUniRule 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 fixation Source: UniProtKB-KW
    2. regulation of nitrogen utilization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Nitrogen fixation

    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
    OrganismiAzospirillum brasilense
    Taxonomic identifieri192 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 933933Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192716Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ8RQD1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini507 – 637131HDUniRule annotationAdd
    BLAST
    Domaini746 – 82984ACT 1UniRule annotationAdd
    BLAST
    Domaini859 – 93375ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 390390UridylyltransferaseAdd
    BLAST
    Regioni391 – 745355Uridylyl-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

    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.

    Q8RQD1-1 [UniParc]FASTAAdd to Basket

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    MLSTRAASAD ASDAKDAGTA NIPNKRAILS RRKLAEDLET LVAEHGTGDK    50
    LRPALIARLR GALNDGRAEV RARFEAKGSG EDCVRQNCYL ADGVVRSLAD 100
    LTVTHIFPTP NPTSGEVFDI VATGGYGRGE LAPFSDIDLL FLLPYKRTPR 150
    VEQVVEYMLY ILWDLGLKVG HAVRSVDDCI RQSKADVTIR TAILESRYLW 200
    GPRKLFHRLR RRFDREVVAG TGPEFVEAKL AERDNRHLKL GDSAYVLEPN 250
    LKDGKGGLRD LQTLFWIAKY LYRVEDVDDL VGKKVLLPEE AHGFAKAQNF 300
    LWTARCHLHY LTGRMEDRMT FDVQTSIGNR MGYTDHAGTK GVERFMKHYF 350
    LVAKDVGDLT RIFCAALEAE SKRPPKFNIL RLAALARRKD VDGFVVDGER 400
    LNVRSDRQFK DEPLDMIRLF HTAQQNDIDI HPNALRAITR SLSVVGPKLR 450
    ADPEANRLFL EILTGRKDPE ITLRRMNEAG VLARFIPDFG RVVAQMQYDM 500
    YHVYTVDEHT LFALGILHKI EMGELTDELP LSSEVIHKVV SRRALYVAVL 550
    LHDIAKGRGG DHSILGARVA EKLCPRLGLT AEETETVAWL VRWHLAMSYT 600
    AFKRDLEDDK TVRDFVSLVQ SPERLRLLLV LTVADIRAVG PQRWNNWKAT 650
    LLRELYNRSE EVMSGGLSVE GRGRRIQAAQ AALRDELSDF DAADFERHLA 700
    LGYPAYWLAF DAETLGRQAR LVRGRLRDER PLTVNTRIDR GRAITEVTIF 750
    ATDHHGLFSR LAGALAAAGA DIVDARIFTM TNGMALDVFT VQDAAGGGAF 800
    ESGDKLAKLS VMIEKVLSGQ LKPLHDLTKR KAPHASRTRV FHVPPRVLID 850
    NNASTTHTVI EVNGRDRPGL LYDLTRALTN LTLQISSAKI STYGEKAIDV 900
    FYVKDVFGLK VTHENKLAQI RERLLHALAD PSA 933
    Length:933
    Mass (Da):104,602
    Last modified:June 1, 2002 - v1
    Checksum:i35E692E0411BB9E7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF149716 Genomic DNA. Translation: AAL87737.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF149716 Genomic DNA. Translation: AAL87737.1 .

    3D structure databases

    ProteinModelPortali Q8RQD1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Cloning and characterization of the Azospirillum brasilense glnD gene and analysis of a glnD mutant."
      Van Dommelen A., Keijers V., Somers E., Vanderleyden J.
      Mol. Gen. Genet. 266:813-820(2002)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.
    2. "Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein."
      Araujo L.M., Huergo L.F., Invitti A.L., Gimenes C.I., Bonatto A.C., Monteiro R.A., Souza E.M., Pedrosa F.O., Chubatsu L.S.
      Braz. J. Med. Biol. Res. 41:289-294(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
      Strain: FP2.

    Entry informationi

    Entry nameiGLND_AZOBR
    AccessioniPrimary (citable) accession number: Q8RQD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 58 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

    Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3