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Q3J5H6

- GLND_RHOS4

UniProt

Q3J5H6 - GLND_RHOS4

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (08 Nov 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 fixation 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. [glutamate-ammonia-ligase] adenylyltransferase activity Source: InterPro
    2. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
    3. amino acid binding Source: InterPro
    4. metal ion binding Source: InterPro
    5. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. nitrogen fixation Source: UniProtKB-HAMAP
    2. regulation of nitrogen utilization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Nitrogen fixation

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciRSPH272943:GJAS-403-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:RHOS4_03900
    ORF Names:RSP_1811
    OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
    Taxonomic identifieri272943 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
    ProteomesiUP000002703: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 930930Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231690Add
    BLAST

    Proteomic databases

    PRIDEiQ3J5H6.

    Interactioni

    Protein-protein interaction databases

    STRINGi272943.RSP_1811.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3J5H6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini505 – 624120HDUniRule annotationAdd
    BLAST
    Domaini742 – 81877ACT 1UniRule annotationAdd
    BLAST
    Domaini852 – 92776ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 387387UridylyltransferaseAdd
    BLAST
    Regioni388 – 741354Uridylyl-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.
    PhylomeDBiQ3J5H6.

    Family and domain databases

    Gene3Di1.10.3210.10. 1 hit.
    HAMAPiMF_00277. PII_uridylyl_transf.
    InterProiIPR002912. ACT_dom.
    IPR010043. GlnD_Uridyltrans.
    IPR005190. GlnE_rpt_dom.
    IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF01842. ACT. 2 hits.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF03710. GlnE. 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.

    Q3J5H6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPASEAGPA QDPLFSGLIL PRSRILDAEA LTRSILAEID AAGPLDPKSA    50
    RAIAVRQMTE AKAAGNRALS ETFEARPREA RGLIRAQAAL TDGLVTAALR 100
    VACERLHPLA NPTEAERIAV LAVGGYGRAE MAPHSDVDLL FLTPWKITPW 150
    AEMVIESMLY MLWDLRLKVG HSSRTVKDCL RLGREDITIR TALLEHRFLA 200
    GHAPLAAELD ETLWNDLFRG TGAEFIDAKL EERGQRHKRQ GGQRYVLEPN 250
    VKEGKGGLRD LQTLYWIGKY LNRVPSPSGL VAAGLLTRDE FETFERAESF 300
    LWAVRCHLHY ATGRATDQLT FDLQVEVAAR MGYADTRGRR GVEVFMQDYF 350
    RHATRVGELT RVFLAQLEAR HEKREPKIMG LFRRKKRLKP EYSLVNGRID 400
    VLDPKAFLAD KLNLLRIFEE ALRTGFLIHP GAMRLIAANL HLIDEEMQHD 450
    REANRIFLDM LLRHGNPERA LRRMNELGVL GAFIPEFERI VAMMQFNVYH 500
    HYTVDEHTIQ CISTLAQIER HELDEELPIA NRILTDGISR RVIYVALLLH 550
    DIGKGRPEDH SILGAQIARR VAPRFGLTAE ECETVEWLVR YHLLMSDMAQ 600
    KRDIGDPRTV RDFAKAVRSK KRLDLLTVLT VCDIRGVGPG TWNNWKAQLL 650
    RKLYRDTVTA LDAGLESLNR ENRADEAKRA LRELLEEWDP KDLRAELARH 700
    YPPYWQALSN ATHAVFARML RGLGETEIRI DLDPDPDRDA TRACFALADH 750
    PGIFSRLAGA LALVGANVVD ARTYTTKDGY ATAVFWIQDS EGSPYEISRL 800
    PRLTSMIDKT LKGEVVAREA LKDRDKLKKR EAQFRFPTHI AFDNEGSDIY 850
    TIIEVDTRDR PGLLYDLTRT LAANNIYIAS AVIATYGAQV VDSFYVKDMF 900
    GLKLHQKNRQ ETLEKKLRQA IVEGAERAKQ 930
    Length:930
    Mass (Da):105,347
    Last modified:November 8, 2005 - v1
    Checksum:iF2C8D050AD54C166
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000143 Genomic DNA. Translation: ABA77958.1.
    RefSeqiYP_351859.1. NC_007493.2.

    Genome annotation databases

    EnsemblBacteriaiABA77958; ABA77958; RSP_1811.
    GeneIDi3719057.
    KEGGirsp:RSP_1811.
    PATRICi23150588. VBIRhoSph57909_0694.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000143 Genomic DNA. Translation: ABA77958.1 .
    RefSeqi YP_351859.1. NC_007493.2.

    3D structure databases

    ProteinModelPortali Q3J5H6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272943.RSP_1811.

    Proteomic databases

    PRIDEi Q3J5H6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABA77958 ; ABA77958 ; RSP_1811 .
    GeneIDi 3719057.
    KEGGi rsp:RSP_1811.
    PATRICi 23150588. VBIRhoSph57909_0694.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261779.
    KOi K00990.
    OMAi LYCLWDM.
    OrthoDBi EOG6CCH44.
    PhylomeDBi Q3J5H6.

    Enzyme and pathway databases

    BioCyci RSPH272943:GJAS-403-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.
    IPR005190. GlnE_rpt_dom.
    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.
    PF03710. GlnE. 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 sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

    Entry informationi

    Entry nameiGLND_RHOS4
    AccessioniPrimary (citable) accession number: Q3J5H6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 65 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