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Q47F95

- GLND_DECAR

UniProt

Q47F95 - GLND_DECAR

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Dechloromonas aromatica (strain RCB)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      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

    BioCyciDARO159087:GI5B-1793-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:Daro_1739
    OrganismiDechloromonas aromatica (strain RCB)
    Taxonomic identifieri159087 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas
    ProteomesiUP000000550: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231681Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi159087.Daro_1739.

    Structurei

    3D structure databases

    ProteinModelPortaliQ47F95.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini437 – 53397HDUniRule annotationAdd
    BLAST
    Domaini676 – 75580ACT 1UniRule annotationAdd
    BLAST
    Domaini784 – 85269ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 317317UridylyltransferaseAdd
    BLAST
    Regioni318 – 675358Uridylyl-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.
    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.

    Q47F95-1 [UniParc]FASTAAdd to Basket

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    MSCDVAALRA EVKANQNQLR LNYEQSNDAV ALLRDRCQHV DTVLEKLWLS    50
    LNFPASLALA AVGGYGRGEL YPASDIDLLI LLPQEASASL QEKLERLVGH 100
    FWDIGLEIGH SVRTVQECLD EAANDITVQT ALLEARLLTG NTKLFATFQK 150
    RLRGNLDPLH FFEAKRLEQQ ERYLRFNETP YSLEPNCKES PGGLRDIQVI 200
    FWIAKAAGYG STWAELHQNG IITQEEMIQM EGCEAYLNHL RIRLHFMLGR 250
    REDRLLFDYQ STLAANYGFV SNEAKRESEQ LMQVYYRNAK TVTVLNTILL 300
    QNMGAALTPE SEQTPQQLDE SFQIVGNLLD IRDEQLYERN PLAILDSFLA 350
    MQESHELFGM TARTLRALWR AREQITPEFR ANPENRAAFM KLLQGDRGIV 400
    HEFRRMNQLG ILGRYLPNFG RIVGQMQHDL FHVYTVDQHI LQVMRNIRRF 450
    TMSEFAHEYP LCSRIISELD RPWLLYVAAL FHDIAKGRGG DHSELGTVDT 500
    REFCVNHGLS EEDTELVVWL VKNHLVMSQV AQKEDLSDPD VIANFIRLVG 550
    DTRHLQALYL LTHADIRGTS PKVWNNWKGK LLADLYYQAI HHINQGEAPA 600
    AHGVIAERQA EAMRLLRFFA LSATVHERLW KQLDTVYFLR HSAEEIAWHT 650
    RSLHYRIYNN QPVVRARPNQ EGDGLQVMVY TQDQPDLFAR IVGFFARAGY 700
    SIVDAKIHTT AHGYALDSFV VLDIEERDND REMVAYIEHE LEQRLLHQMP 750
    RDVPSSGRLS RQVKHFPIKP EVSIRGDEKG THFILSLVAA DRPGLLYTVA 800
    NTLTEHGAYL HTAKITTLGE RAEDVFLISG GDLRDTHNRI RLETELMERL 850
    KV 852
    Length:852
    Mass (Da):97,701
    Last modified:September 13, 2005 - v1
    Checksum:iB60B7794DE1B3594
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000089 Genomic DNA. Translation: AAZ46486.1.
    RefSeqiYP_284956.1. NC_007298.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ46486; AAZ46486; Daro_1739.
    GeneIDi3568481.
    KEGGidar:Daro_1739.
    PATRICi21602120. VBIDecAro89105_1724.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000089 Genomic DNA. Translation: AAZ46486.1 .
    RefSeqi YP_284956.1. NC_007298.1.

    3D structure databases

    ProteinModelPortali Q47F95.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 159087.Daro_1739.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ46486 ; AAZ46486 ; Daro_1739 .
    GeneIDi 3568481.
    KEGGi dar:Daro_1739.
    PATRICi 21602120. VBIDecAro89105_1724.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci DARO159087:GI5B-1793-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. "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
      Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
      BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RCB.

    Entry informationi

    Entry nameiGLND_DECAR
    AccessioniPrimary (citable) accession number: Q47F95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 67 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