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Q5FPT6

- GLND_GLUOX

UniProt

Q5FPT6 - GLND_GLUOX

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Mar 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

    BioCyciGOXY290633:GHB3-1870-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:GOX1872
    OrganismiGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
    Taxonomic identifieri290633 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter
    ProteomesiUP000006375: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 949949Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192735Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi290633.GOX1872.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5FPT6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini541 – 62989HDUniRule annotationAdd
    BLAST
    Domaini757 – 83478ACT 1UniRule annotationAdd
    BLAST
    Domaini870 – 94980ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 395395UridylyltransferaseAdd
    BLAST
    Regioni396 – 756361Uridylyl-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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF01842. ACT. 2 hits.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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.

    Q5FPT6-1 [UniParc]FASTAAdd to Basket

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    MKETSFWGET PSLSFADDTD KPLSDRTASP PCDPASSLQT ALDTAAAQGQ    50
    TTRENVLSIL RRHLGSGNAT VRREFEKRRM SGIDAARALA RQADDMVCAL 100
    AELAAQKHES PGETLCLCAT GGYGAGLLAP FSDIDILFLI PGDPTPAMTA 150
    RIEFILYALW DLGLRVGHAT RSIAECVRDA DSDLTIRTAL LDLRFLHGER 200
    GLARDLRCAL GADLQNDRLC EFVMGKIAER EQRHRRFGDN PYMVEPNIKE 250
    GRGGLRDLQT LNWMGRAALG CAVSTPDRSG QPAEAPQTPS FASFGLLTDR 300
    ESLRARRSWD FLWTVRLHLH YITGRAEERL TFDVQPVIGG RMGYATHGRQ 350
    RGVERFMRHY FLTARDVMRL TSVLQPVVLM HLQDQTTGEP PKVVPGPEEF 400
    QTIAGRICPI EPVTFAAQPR EMFRLLDCGR RHDLPLHPIA MQQIIRNERH 450
    AVTLRDDPET AKIFLDLLCE PSADETKAVP FWLPILNETG LLGRLLPDWS 500
    RVVGQMQFDS YHIYTVDEHI VEAVRMMGQI EAGRMADEIP LAYTLASDLR 550
    SRRALYVAVL LHDIGKGRGG DHSEIGADLA LTICPQLGLD PEETDTVSWL 600
    VLHHLLLSQT AFTRDIDDPR TILDLADTIQ SPERLRLLLL LTIADMRAVS 650
    PKVWNAWKAT LLRELFSRVA EVLEGGLAAT ERDSRVNHAR ELARDGLTGI 700
    LPESSIDRFL DLGYPSYWLG FDTDTQMRHA RMVHDSDRYR SPVTVEAYPI 750
    PERGVTELTV LCADHPGLFS QIAGALAVSG ASIVDARIHT LSDGMALDTF 800
    WVQDGEGCSF EEPHQLGRLN HLVEQALSGR LDIRKGIEDA SHHSTSRRMR 850
    AIHVPPRVVI DNTASDRHTV IEVNGRDRPG LLHDVTSALS SASLQISSAH 900
    ITTYGMRAVD VFYVRDLLGM KITDPVRLAR LRETLLASLT SAPVTTPAS 949
    Length:949
    Mass (Da):105,398
    Last modified:March 1, 2005 - v1
    Checksum:i79BEEE7485522A9B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000009 Genomic DNA. Translation: AAW61610.1.
    RefSeqiYP_192266.1. NC_006677.1.

    Genome annotation databases

    EnsemblBacteriaiAAW61610; AAW61610; GOX1872.
    GeneIDi3250631.
    KEGGigox:GOX1872.
    PATRICi32611646. VBIGluOxy81109_2161.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000009 Genomic DNA. Translation: AAW61610.1 .
    RefSeqi YP_192266.1. NC_006677.1.

    3D structure databases

    ProteinModelPortali Q5FPT6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 290633.GOX1872.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW61610 ; AAW61610 ; GOX1872 .
    GeneIDi 3250631.
    KEGGi gox:GOX1872.
    PATRICi 32611646. VBIGluOxy81109_2161.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci GOXY290633:GHB3-1870-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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view ]
    Pfami PF01842. ACT. 2 hits.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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. "Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
      Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
      Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 621H.

    Entry informationi

    Entry nameiGLND_GLUOX
    AccessioniPrimary (citable) accession number: Q5FPT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: March 1, 2005
    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