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Q02RD0

- GLND_PSEAB

UniProt

Q02RD0 - GLND_PSEAB

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (14 Nov 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

    BioCyciPAER208963:GI5K-1370-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:PA14_17040
    OrganismiPseudomonas aeruginosa (strain UCBPP-PA14)
    Taxonomic identifieri208963 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000000653: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022350Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi208963.PA14_17040.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02RD0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini463 – 569107HDUniRule annotationAdd
    BLAST
    Domaini706 – 78984ACT 1UniRule annotationAdd
    BLAST
    Domaini816 – 89176ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 342342UridylyltransferaseAdd
    BLAST
    Regioni343 – 705363Uridylyl-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.
    HOGENOMiHOG000261778.
    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.
    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.

    Q02RD0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPQVDPELFD RGQFQAELAL KSSPIAAFKK AIRQFREVLD NRFNSGRDIR    50
    RLIEDRAWCV DQILQQAWQR FDWGDDADIT LVAVGGYGRG ELHPYSDVDL 100
    LILLDSEDQE SFREPIEGFL TLLWDIGLEV GQSVRSVQQC AEEARADLTV 150
    ITTLMECRTI CGPDSLRQRM LQVTGSAHMW PSKEFFLAKR HEQQRRHAKY 200
    NDTEYNLEPN VKGSPGGLRD IQTILWMARR QFGSLNLHAL VREGFLVESE 250
    CSMLASSQEF LWRVRYALHM LAGRAEDRLL FDHQRSIARL FGYEDNDVKL 300
    AVERFMQKYY RVVMAISELN DLIIQHFEEV ILPCEQPVQI QPLNSRFQLR 350
    DGYIEVTHPN VFKRTPFALL EIFVLMAQHP EIKGVRADTI RLLRDSRHLI 400
    DDEFRHDIRN TSLFIELFKS SQGIHRNLRR MNRYGILGRY LPEFGHIIGQ 450
    MQHDLFHIYT VDAHTLNLIK HLRKLNRPEM AEKYPLASKI IDRLPKPELI 500
    YIAGLYHDIA KGRGGDHSEL GAVDAEAFCQ SHQLPPWDTQ LVSWLVQNHL 550
    VMSTTAQRKD LSDPQVIFDF AQLVGDQTHL DYLYVLTVAD INATNPTLWN 600
    SWRASLLRQL YTETKRALRR GLENPVDREE QIRQTQTAAL DQLVRNGIDQ 650
    DDAEQLWSQL GDDYFLRHTA GDVAWHTEAI LQHPDDGTPL VLIKETTQRE 700
    FESGSQIFIY AADQHDFFAV TVAAMDQLNL SIQDARIITS TSQFTLDTYI 750
    VLDADGDSIG NNPERIAEIR EGLIDALKNP DDYPTIIQRR VPRQLKHFAF 800
    APQVTISTDA LRQVSVLEVI APDRPGLLAR IGGIFLDFDL SVQNAKIATL 850
    GERVEDVFYI TDARNQPLAD PDLCKRLQAA LVEQLSQDNG RDTLPTRINF 900
    Length:900
    Mass (Da):103,418
    Last modified:November 14, 2006 - v1
    Checksum:i3CD9887250E5E897
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000438 Genomic DNA. Translation: ABJ12891.1.
    RefSeqiYP_789506.1. NC_008463.1.

    Genome annotation databases

    EnsemblBacteriaiABJ12891; ABJ12891; PA14_17040.
    GeneIDi4383349.
    KEGGipau:PA14_17040.
    PATRICi19848829. VBIPseAer79785_1386.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000438 Genomic DNA. Translation: ABJ12891.1 .
    RefSeqi YP_789506.1. NC_008463.1.

    3D structure databases

    ProteinModelPortali Q02RD0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208963.PA14_17040.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABJ12891 ; ABJ12891 ; PA14_17040 .
    GeneIDi 4383349.
    KEGGi pau:PA14_17040.
    PATRICi 19848829. VBIPseAer79785_1386.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261778.
    KOi K00990.
    OMAi HHLLMSV.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci PAER208963:GI5K-1370-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: UCBPP-PA14.

    Entry informationi

    Entry nameiGLND_PSEAB
    AccessioniPrimary (citable) accession number: Q02RD0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 14, 2006
    Last modified: October 1, 2014
    This is version 60 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3