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B4RC79

- GLND_PHEZH

UniProt

B4RC79 - GLND_PHEZH

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Phenylobacterium zucineum (strain HLK1)
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 (23 Sep 2008)
      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

    BioCyciPZUC450851:GHUG-3508-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:PHZ_c3463
    OrganismiPhenylobacterium zucineum (strain HLK1)
    Taxonomic identifieri450851 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaePhenylobacterium
    ProteomesiUP000001868: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 938938Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000114757Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi450851.PHZ_c3463.

    Structurei

    3D structure databases

    ProteinModelPortaliB4RC79.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini496 – 624129HDUniRule annotationAdd
    BLAST
    Domaini734 – 81380ACT 1UniRule annotationAdd
    BLAST
    Domaini845 – 92480ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 379379UridylyltransferaseAdd
    BLAST
    Regioni380 – 733354Uridylyl-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.
    OMAiLYCLWDM.
    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.

    B4RC79-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPRLRPTHL EYVVDGVKLR SQLSAAALEH AGDELAQRRA ALEILKNALF    50
    RGRMIAKERL ENGAGGIETA RLLSGVTDEV VSALYDFTTV HVFRARNPTE 100
    GERLALMAVG GYGRGTLAPF SDIDLLFVRP YKQTAHAESV IEYMLYALWD 150
    LGFKVGHASR TIDECLKLSR EDFTIRTSIL EARRLTGDEK LAGELVERFR 200
    KEVVKGTGAE FVAAKLKERD ERHARAGASR YMVEPNVKEG KGGLRDLNTL 250
    FWIAQYLHPG ESLEKVMHLE IFDRREVRTF IQALDFLWAV RCHLHFATGR 300
    PEERLSFDLQ PEIARRMGYG DRGDAPAVER FMRRYFLFAK DVGSLTRVFA 350
    AKLEADRVKT APKGISRFIP GRAQKRKPLD EPGFHEVGGR LGVDPEIFEA 400
    DPVNLLKLFR IADQRNLDLH PDAFTAASRA SGLITSAVRR DRHAAKVFLD 450
    ILARGRDPQR TLALMNEAGV LGRFVPEFGR IVAQMQFNMY HSYTVDEHTL 500
    RAVGVIADIA AGRLAEDHPL AVQTMPLIAD REALFLAMLL HDTGKGGAGG 550
    QELAGARAAR QACERLGLER SKIELVAWLV EHHLVMSDYA QKRDVSDPRT 600
    VADFARIVQS PERLRLLLVL TVADIRAVGP GVWNGWKGQL MRELYTATEA 650
    VFRGGRGSDA AAALKRYQEN AAYDARVSLA KADPLAEPWA DAMEDAYFTA 700
    FSEAEVLAHA RLAQQAGGGA AAEGRIRSEL NAAEVVVAAA DRPRLFVDLA 750
    EAITAAGANV MGARVFTSRA GQALDVFYVQ DASGQPFGSH DPRALARLAE 800
    TLACAARGEP VAREPRKPQD LGRTAAFAIT PAVMLDNEAS ETSTVVEASG 850
    RDRPGLLAAL ARTISDAGLS ILSAHIDGYG ERAVDAFYVV DADGRKLTDA 900
    RKRNALKSAL LAALTKAEAE TAQARRTNLQ RARASVAR 938
    Length:938
    Mass (Da):102,982
    Last modified:September 23, 2008 - v1
    Checksum:i4D684D54FEEEB95E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000747 Genomic DNA. Translation: ACG79872.1.
    RefSeqiYP_002132301.1. NC_011144.1.

    Genome annotation databases

    EnsemblBacteriaiACG79872; ACG79872; PHZ_c3463.
    GeneIDi6789416.
    KEGGipzu:PHZ_c3463.
    PATRICi22930318. VBIPheZuc44517_4213.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000747 Genomic DNA. Translation: ACG79872.1 .
    RefSeqi YP_002132301.1. NC_011144.1.

    3D structure databases

    ProteinModelPortali B4RC79.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 450851.PHZ_c3463.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACG79872 ; ACG79872 ; PHZ_c3463 .
    GeneIDi 6789416.
    KEGGi pzu:PHZ_c3463.
    PATRICi 22930318. VBIPheZuc44517_4213.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PZUC450851:GHUG-3508-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. "Complete genome of Phenylobacterium zucineum - a novel facultative intracellular bacterium isolated from human erythroleukemia cell line K562."
      Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.
      BMC Genomics 9:386-386(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HLK1.

    Entry informationi

    Entry nameiGLND_PHEZH
    AccessioniPrimary (citable) accession number: B4RC79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: September 23, 2008
    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