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Q9Z9H0

- GLND_PSEAE

UniProt

Q9Z9H0 - GLND_PSEAE

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (08 Dec 2000)
      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

    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:PA3658
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA3658.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192752Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi208964.PA3658.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z9H0.
    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.
    PhylomeDBiQ9Z9H0.

    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.

    Q9Z9H0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPQVDPELFD RGQFQAELAL KSSPIAAFKK AIRQFREVLD NRFNSGRDIR    50
    RLIEDRAWCV DQILQQAWQR FDWGDDADIA 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 SHQLPLWDTQ 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):103,404
    Last modified:December 8, 2000 - v2
    Checksum:i7C71F31EC284E836
    GO

    Sequence cautioni

    The sequence BAA75913.1 differs from that shown. Reason: Frameshift at position 285.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti811 – 8111L → V in BAA75913. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024601 Genomic DNA. Translation: BAA75913.1. Frameshift.
    AE004091 Genomic DNA. Translation: AAG07046.1.
    PIRiE83189.
    RefSeqiNP_252348.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG07046; AAG07046; PA3658.
    GeneIDi880565.
    KEGGipae:PA3658.
    PATRICi19841939. VBIPseAer58763_3827.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024601 Genomic DNA. Translation: BAA75913.1 . Frameshift.
    AE004091 Genomic DNA. Translation: AAG07046.1 .
    PIRi E83189.
    RefSeqi NP_252348.1. NC_002516.2.

    3D structure databases

    ProteinModelPortali Q9Z9H0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA3658.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG07046 ; AAG07046 ; PA3658 .
    GeneIDi 880565.
    KEGGi pae:PA3658.
    PATRICi 19841939. VBIPseAer58763_3827.

    Organism-specific databases

    PseudoCAPi PA3658.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261778.
    KOi K00990.
    OMAi HHLLMSV.
    OrthoDBi EOG6CCH44.
    PhylomeDBi Q9Z9H0.

    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. Nashimoto H.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiGLND_PSEAE
    AccessioniPrimary (citable) accession number: Q9Z9H0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: December 8, 2000
    Last modified: October 1, 2014
    This is version 98 of the entry and version 2 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