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Q2N784

- GLND_ERYLH

UniProt

Q2N784 - GLND_ERYLH

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Erythrobacter litoralis (strain HTCC2594)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (07 Feb 2006)
      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

    BioCyciELIT314225:GHLE-2407-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:ELI_11825
    OrganismiErythrobacter litoralis (strain HTCC2594)
    Taxonomic identifieri314225 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter
    ProteomesiUP000008808: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 919919Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022343Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi314225.ELI_11825.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2N784.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini490 – 592103HDUniRule annotationAdd
    BLAST
    Domaini728 – 81184ACT 1UniRule annotationAdd
    BLAST
    Domaini839 – 91981ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 373373UridylyltransferaseAdd
    BLAST
    Regioni374 – 727354Uridylyl-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.
    IPR005105. GlnD_Uridyltrans_N.
    IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF03445. DUF294. 1 hit.
    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.

    Q2N784-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDPKVPRQR RIIDRRKLAA AVEALAEQQG EKARPAVLKV LREALEKGRD    50
    ELSQRLLDRP SAGHQITAGH AFLVDQLVRV IFDHVTTHLY PVANRSSSER 100
    IAVLAVGGYG RAEMAPQSDV DIAFLHPSRR TPWCEQVTEA MLYFLWDLGF 150
    KVGQSSRTPE DMVRMAREDL TIRTALLEAR FVWGDRELYD EARKRFWSEV 200
    VNGTERQFVA EKLAERDARH ERMGGTRYVV EPNVKEGKGG LRDLQTLYWI 250
    GKYIHRARGA AELVDAGLLT ETEYHGFRRA EGFLLAVRCH LHEITGRPED 300
    RLTFDFQKQI AERMRFAERR EKSAVERFMQ YYFLQVKRVG SLTGVFLAQM 350
    DQQFARKRAR TGLLAGFNAK SRMLKGYTVF GGKIAAPGDN WFRDDPVRLI 400
    EIFQLAEANG LEIDPRSMRQ ADRDSVLIKD QVRNDPRANA IFLDLLCGRN 450
    DPETALRWMN EAGVFGKFVP DFGRVNAQMQ FNMYHHYTVD EHTIRAIGFL 500
    SKIEKGELAK EHPRSTREIH KVKSRRVAFV AALLHDIAKG RGGDHSILGA 550
    EVAEELCPRF GLDEDETDLV AWLVLQHLLM SSTAQKRDLT DPKTIEDFVA 600
    EVQSLERLRH LAILTSVDIR AVGPGTWNSW KGQLLGELYD AAHERLRLGH 650
    MKHHRSERVA AKKEAVREAL GGKAALLEKH GRLLPDSYWI AEPENVISRN 700
    IVQYDVAREI SEDLSIHCEF DEERGATLVT VIAADHPGLF YRIAGGIHLA 750
    GGNIIDARIH TTRNGWAIDN YLVQDPVGQP FAEERQLARI EQAIADAIAN 800
    RGELVPKLAK RPLKQTRAGA FDVRPRVLFD NDASGRFTVI EVNARDRAAL 850
    LNRLGRALFE NQVIVQSAHI TAYGERAADT FYVTDLTGAK ITDESRMDTI 900
    RQALLDAASD ARQAELEPA 919
    Length:919
    Mass (Da):104,003
    Last modified:February 7, 2006 - v1
    Checksum:iB532D60CE3188D12
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000157 Genomic DNA. Translation: ABC64457.1.
    RefSeqiYP_459254.1. NC_007722.1.

    Genome annotation databases

    EnsemblBacteriaiABC64457; ABC64457; ELI_11825.
    GeneIDi3871505.
    KEGGieli:ELI_11825.
    PATRICi21861869. VBIEryLit102657_2349.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000157 Genomic DNA. Translation: ABC64457.1 .
    RefSeqi YP_459254.1. NC_007722.1.

    3D structure databases

    ProteinModelPortali Q2N784.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 314225.ELI_11825.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABC64457 ; ABC64457 ; ELI_11825 .
    GeneIDi 3871505.
    KEGGi eli:ELI_11825.
    PATRICi 21861869. VBIEryLit102657_2349.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci ELIT314225:GHLE-2407-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.
    IPR005105. GlnD_Uridyltrans_N.
    IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view ]
    Pfami PF03445. DUF294. 1 hit.
    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 Erythrobacter litoralis HTCC2594."
      Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
      J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HTCC2594.

    Entry informationi

    Entry nameiGLND_ERYLH
    AccessioniPrimary (citable) accession number: Q2N784
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 59 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