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P62223

- GLND_RHOPA

UniProt

P62223 - GLND_RHOPA

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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. [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 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

    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:RPA0591
    OrganismiRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
    Taxonomic identifieri258594 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
    ProteomesiUP000001426: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 929929Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192762Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    IntActiP62223. 1 interaction.
    MINTiMINT-6732844.
    STRINGi258594.RPA0591.

    Structurei

    3D structure databases

    ProteinModelPortaliP62223.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini497 – 59296HDUniRule annotationAdd
    BLAST
    Domaini736 – 81883ACT 1UniRule annotationAdd
    BLAST
    Domaini849 – 92981ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 379379UridylyltransferaseAdd
    BLAST
    Regioni380 – 735356Uridylyl-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.
    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. 2 hits.
    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.

    P62223-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPSRPAADE RFDSARVAAE IATLAEKHTG NDAAFRTALA MLMKAELAKA    50
    RTEAEAQLLR DRHGRRCAER LCYVQDAIIR LLFNAATEYL YNTPTPSSSE 100
    RMTVVATGGY GRGLMAPESD IDLLFILPYK QTAWGEQVAE VILYCLWDIG 150
    LKVGHATRSV DECIRQARAD MTIRTAILET RFLAGDEALY AELVERFDKE 200
    VVEGTAAEFV AAKLAEREER HRRSGQSRYL VEPNVKDGKG GLRDLHTLFW 250
    IAKYVYRVRE ASELSERGVF DPAEFRTFRR CEDFLWSVRC NIHFVTKRAE 300
    DRLSFDLQRE IGVRLGYTSH PGMQDVERFM KHYFLIAKEV GNLTAILCAK 350
    LEDQQAKAAP ALTRMMARLR PAAKRRRVPE SDDFVIDNNR INLAVPDVFK 400
    HDPVNLIRIF RLAQKNNLAF HPDAMRSVTR SLSLITPQLR DNPEANRLFV 450
    EILTSDNAEP VLRRMNETGV LGRFIRAFGR IVSMMQFNMY HSYTVDEHLI 500
    RCVGNLQEIE RGGNDEFALS SELIRKIRPD HRAVLYAAVL LHDIAKGQPE 550
    DHSTAGAKVA RRLCPRFGFS TADTELVAWL IEKHLVMSTV AQSRDLSDRK 600
    TIENFAAVVE TVEQMKMLTI LTTADIRGVG PGVWNGWKAQ LIRTLYYETE 650
    PVLTGGFSEV NRAERIRAAQ AEFRAAFTEW PEADLNAYVA RHYPAYWLKV 700
    DLQRKIRHAR FLRASEQAGH KLAINVGFDE ARAVTELTIL AVDHPWLLSV 750
    IAGACASAGA NIVDAQIYTT TDGRALDTIS ISREYDRDED EGRRATRIGE 800
    TIEEVLEGKL RLPEAVARRA SSGSKAKLRA FVVEPEVEIN NNWSDRYTVI 850
    EVSGLDRPGL LYQLTTAISK LNLNIASAHV ATFGERARDV FYVTDLLGAQ 900
    ITAPTRQAAI KRALVHLLAN GDAAEKPAA 929
    Length:929
    Mass (Da):104,542
    Last modified:July 5, 2004 - v1
    Checksum:iBC13BFA4845F8785
    GO

    Sequence cautioni

    The sequence CAE26035.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX572594 Genomic DNA. Translation: CAE26035.1. Different initiation.
    RefSeqiNP_945944.1. NC_005296.1.

    Genome annotation databases

    EnsemblBacteriaiCAE26035; CAE26035; RPA0591.
    GeneIDi2692917.
    KEGGirpa:RPA0591.
    PATRICi23285359. VBIRhoPal84835_0625.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX572594 Genomic DNA. Translation: CAE26035.1 . Different initiation.
    RefSeqi NP_945944.1. NC_005296.1.

    3D structure databases

    ProteinModelPortali P62223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P62223. 1 interaction.
    MINTi MINT-6732844.
    STRINGi 258594.RPA0591.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE26035 ; CAE26035 ; RPA0591 .
    GeneIDi 2692917.
    KEGGi rpa:RPA0591.
    PATRICi 23285359. VBIRhoPal84835_0625.

    Phylogenomic databases

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

    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. 2 hits.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-98 / CGA009.

    Entry informationi

    Entry nameiGLND_RHOPA
    AccessioniPrimary (citable) accession number: P62223
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 70 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