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Q1QDM9

- GLND_PSYCK

UniProt

Q1QDM9 - GLND_PSYCK

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Psychrobacter cryohalolentis (strain K5)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (16 May 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

    BioCyciPCRY335284:GHE9-456-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:Pcryo_0441
    OrganismiPsychrobacter cryohalolentis (strain K5)
    Taxonomic identifieri335284 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
    ProteomesiUP000002425: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 913913Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022352Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi335284.Pcryo_0441.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1QDM9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini479 – 586108HDUniRule annotationAdd
    BLAST
    Domaini730 – 81586ACT 1UniRule annotationAdd
    BLAST
    Domaini838 – 91376ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 358358UridylyltransferaseAdd
    BLAST
    Regioni359 – 729371Uridylyl-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.

    Q1QDM9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFNCDVTAID LTPMPLFSAD NMTTAFLSTD TSVVEKSLFG IPEWLLQIND    50
    DISRALERGV NIRQLVSARA CVIDDLLIEL FKCFGLDKTD LALFATGGYG 100
    RGELSLHSDI DILLLMPHDI NADTSSKIDN LVALLWDIGL EPALSVRSVS 150
    DCLEAALDHT IASALLEARL LIGNDALQNV PHQIVNNQWS PRSFYDVKID 200
    EAKARYLQHN ATEYNLEPNI KTAPGGLRDI HIIGWVTKRY FRVSKLYDLV 250
    QQNFLTEKEF DELSFSENYL WQIRHYLHEL TGRNENKLLF DYQREIAQLM 300
    GYDTQTDDQP NAAVERFMRD YYRCAMQIST LSEMLTNHYY ETIIEAQLPD 350
    EERPKKQPIN ARFNQVGDQI AMAHHRVFAQ HPESILEMFL LMGQYGIKNV 400
    RTHTLRALKI AARGIDQAYR DNPTHQTLFL ANLKEQNYLF HRLRTMNRYG 450
    VLGNYIPAFA QVTGLMQYDL FHRYTVDAHT LFLIRILHRF TDPHFYEDFP 500
    LVSSIFQRIE RKEILVLAAM FHDIAKGRGG NHSQLGEIES IEFCLAHGMS 550
    TADANLVGWL TRYHLLMSMT AQKKDISDPE VVTLFADLVG NVTHLNHLYV 600
    LTVADMNATN PQLWNSWRAT LMKQLYSQTR RILRADIDAP TNRQDMISAT 650
    RKQALVMLDN VDNQHMNRDE VLRLWDDLGD EYFLREIAED ILWHTEAILN 700
    HPPIGRASNA DSPPLVVLRE HRELALDAVQ VFVYTQDQVN LFAVTMAVFD 750
    QMNLDVLDAR IITATRDFAL DSYVLLDRSG TLLVDSDSQQ ELKQRLIDAF 800
    KNPTAPKLTH KRIPRQLKHF DVATTINFDF NDASNQHIMS LETLDQPGLL 850
    ARVGQVFLQQ QIEVHAARIT TLGERAEDMF YISDQNDQAL SADKLKTLKT 900
    ALIDSLSVRN DRV 913
    Length:913
    Mass (Da):104,638
    Last modified:May 16, 2006 - v1
    Checksum:i1E1118BBFD987E10
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000323 Genomic DNA. Translation: ABE74224.1.
    RefSeqiYP_579708.1. NC_007969.1.

    Genome annotation databases

    EnsemblBacteriaiABE74224; ABE74224; Pcryo_0441.
    GeneIDi4034059.
    KEGGipcr:Pcryo_0441.
    PATRICi23060331. VBIPsyCry128170_0505.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000323 Genomic DNA. Translation: ABE74224.1 .
    RefSeqi YP_579708.1. NC_007969.1.

    3D structure databases

    ProteinModelPortali Q1QDM9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 335284.Pcryo_0441.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE74224 ; ABE74224 ; Pcryo_0441 .
    GeneIDi 4034059.
    KEGGi pcr:Pcryo_0441.
    PATRICi 23060331. VBIPsyCry128170_0505.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PCRY335284:GHE9-456-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. "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.
      , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K5.

    Entry informationi

    Entry nameiGLND_PSYCK
    AccessioniPrimary (citable) accession number: Q1QDM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 63 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