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Q4FUP5

- GLND_PSYA2

UniProt

Q4FUP5 - GLND_PSYA2

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (30 Aug 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 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

    BioCyciPARC259536:GI3A-410-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:Psyc_0395
    OrganismiPsychrobacter arcticus (strain DSM 17307 / 273-4)
    Taxonomic identifieri259536 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
    ProteomesiUP000000546: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 915915Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231688Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi259536.Psyc_0395.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4FUP5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini498 – 58891HDUniRule annotationAdd
    BLAST
    Domaini732 – 81786ACT 1UniRule annotationAdd
    BLAST
    Domaini840 – 91576ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 360360UridylyltransferaseAdd
    BLAST
    Regioni361 – 731371Uridylyl-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.

    Q4FUP5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFNCAVTAID LTPMPLLSTD NMTTAPLSLS TDTSLIEKSL FGIPEWLLQI    50
    NDDISRALER GVNIRQLVSA RACVIDDLLI GLFKWFELDK TDLALFATGG 100
    YGRGELSLHS DIDILLLMPH EIDADTSSKI DNLVALLWDI GLEPALSVRS 150
    VSECLEAALD HTIASALLEA RLLIGNETLQ DVPHQIVNNQ WSPRAFYDVK 200
    IDEAKARYLQ HNATEYNLEP NIKTAPGGLR DIHIVGWVTK RYFRVSKLYD 250
    LVQQNFLTEK EFDELSFSEG YLWQIRHYLH ELTGRNENKL LFDYQREIAQ 300
    LMGYDTQPDD QPNAAVERFM RDYYRCAMQI STLSEMLTNH YYETIIEPQL 350
    PDEERPKKQP INARFNQVGE QIAMAHHRVF AQHPESILEM FLLMGQYGIK 400
    NVRTHTLRAL KIAARGIDQA YRDNPTHQTL FLANLKEQNY LFHRLRTMNR 450
    YGVLGNYIPA FAQVTGLMQY DLFHRYTVDA HTLFLIRILH RFIDPHFYED 500
    FPLVSSIFQR IERKEILVLA AMFHDIAKGR GGNHSQLGEI ESIEFCLAHG 550
    MSNADANLVG WLTRYHLLMS MTAQKKDISD PEVVTLFADL VGNVTHLNHL 600
    YVLTVADMNA TNPQLWNSWR ATLMKQLYSQ TRRILRADID APTNRQDMIS 650
    ATRKQALMML DNVDNQHMNR DEVLSLWDDL GDEYFLREIA EDILWHTEAI 700
    LNHPPIGRAS NADSPPLVVL REHRELALDA VQVFVYTQDQ VNLFAVTMAV 750
    FDQMNLDVLD ARIITATRDF ALDSYVLLDR SGTLLVDSDS QQELKQRLID 800
    AFKNPTAPKL THKRIPRQLK HFDVETTINF EFNDASSQHI MSLETLDQPG 850
    LLARVGQVFL QQQIEVHAAR ITTLGERAED MFYISDQNDQ ALSANKLKTL 900
    KTALIESLSV HNDSI 915
    Length:915
    Mass (Da):104,846
    Last modified:August 30, 2005 - v1
    Checksum:i68837CAE3D605366
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000082 Genomic DNA. Translation: AAZ18263.1.
    RefSeqiYP_263697.1. NC_007204.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ18263; AAZ18263; Psyc_0395.
    GeneIDi3514133.
    KEGGipar:Psyc_0395.
    PATRICi23055115. VBIPsyArc98534_0490.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000082 Genomic DNA. Translation: AAZ18263.1 .
    RefSeqi YP_263697.1. NC_007204.1.

    3D structure databases

    ProteinModelPortali Q4FUP5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 259536.Psyc_0395.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ18263 ; AAZ18263 ; Psyc_0395 .
    GeneIDi 3514133.
    KEGGi par:Psyc_0395.
    PATRICi 23055115. VBIPsyArc98534_0490.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PARC259536:GI3A-410-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. "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
      Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
      Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 17307 / 273-4.

    Entry informationi

    Entry nameiGLND_PSYA2
    AccessioniPrimary (citable) accession number: Q4FUP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 64 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