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B9JZI2

- GLND_AGRVS

UniProt

B9JZI2 - GLND_AGRVS

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain S4))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (24 Mar 2009)
      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

    BioCyciAVIT311402:GH2Y-338-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:Avi_0424
    OrganismiAgrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain S4))
    Taxonomic identifieri311402 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium
    ProteomesiUP000001596: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 941941Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000132525Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi311402.Avi_0424.

    Structurei

    3D structure databases

    ProteinModelPortaliB9JZI2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini517 – 60488HDUniRule annotationAdd
    BLAST
    Domaini729 – 81082ACT 1UniRule annotationAdd
    BLAST
    Domaini840 – 91980ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 372372UridylyltransferaseAdd
    BLAST
    Regioni373 – 728356Uridylyl-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. 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.

    B9JZI2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKHDLSDAT LPDFKALEAE CMSIVLQNGK VPETRAAILP LLKKASIDGR    50
    EAALRHLTTN GSGLECAGMI SNLQDNLITL VHRMVTQAVY PTTQQEFAVA 100
    AVGGYGRSTL APGSDIDLLF LLSVKAGADA RKAVEFLLYI LWDLGFKVGH 150
    ATRLVEECIR LSRTDMTIRT AILETRFICG EALLVGELQK RFDAEVVEKT 200
    APEFIAAKLA ERDERHRKAG DTRYLVEPNV KEGKGGLRDL HTLFWIAKYY 250
    YRISDPADLV KLGVLSRQEW RMFQKSDDFL WAVRCHMHFA TGKPEERLSF 300
    DLQPEIARNL GYNARPGLSE VERFMKHYFH VAKNVGDLTR IVCASLEDKQ 350
    AKAAPGLTAA IGRFAHRPRR IPGTPEFIED RGRIALSGPD IFKRDPINIM 400
    RFFHVADLHG LEFHPDALKA ITRCLPLIDH DFRENEEANR LFLSILTSKR 450
    DPALMLTRMN EAGVLGKFIP DFGRIVSMMQ FNMYHHYTVD EHLIRSVGIL 500
    AEVDQGQHAD IHPLAVKLMP NIEERTVLFV AVLLHDIAKG RQEDHSIAGA 550
    KVARRLCPRL GLNDKQTELV VWLIDQHLLM SMVAQTRDLH DRKTITDFAE 600
    KVQSLDRLRM LLVLTVCDIR AVGPGVWNGW KGQLLRTLYY ETELLLSGGF 650
    SESPRKERAK QAAEQLAEAL SDWSQKDQKT YTKLHYQPYL LTVPLEDQVR 700
    HAHFIRQADK ADQALATMVR THSFHAITEI TVLAPDHPRL LSIIAGACAA 750
    AGANIADAQI FTTSDGRALD TILINREFPI DEDEMRRANT ISKMIEDVLA 800
    GKKRLPEVIA TRTKGRKRNK TFTVKPHVTI SNSLSNKFTV IEIECLDRIG 850
    LLAEVTAVLA DLSLDIHSAR ITTFGEKVID TFYVIDLVGQ KITNENRQGS 900
    ISVRLKAVMS EQPDELREQM PSGIIAPAAT KSPAAEKKAR V 941
    Length:941
    Mass (Da):105,604
    Last modified:March 24, 2009 - v1
    Checksum:i66E7CBB0A01D8CDB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000633 Genomic DNA. Translation: ACM35294.1.
    RefSeqiYP_002548298.1. NC_011989.1.

    Genome annotation databases

    EnsemblBacteriaiACM35294; ACM35294; Avi_0424.
    GeneIDi7388439.
    KEGGiavi:Avi_0424.
    PATRICi20825788. VBIAgrVit37146_2575.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000633 Genomic DNA. Translation: ACM35294.1 .
    RefSeqi YP_002548298.1. NC_011989.1.

    3D structure databases

    ProteinModelPortali B9JZI2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 311402.Avi_0424.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACM35294 ; ACM35294 ; Avi_0424 .
    GeneIDi 7388439.
    KEGGi avi:Avi_0424.
    PATRICi 20825788. VBIAgrVit37146_2575.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci AVIT311402:GH2Y-338-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: S4 / ATCC BAA-846.

    Entry informationi

    Entry nameiGLND_AGRVS
    AccessioniPrimary (citable) accession number: B9JZI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 44 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