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A5WCX0

- GLND_PSYWF

UniProt

A5WCX0 - GLND_PSYWF

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Psychrobacter sp. (strain PRwf-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (10 Jul 2007)
      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

    BioCyciPPRW349106:GHZF-566-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:PsycPRwf_0556
    OrganismiPsychrobacter sp. (strain PRwf-1)
    Taxonomic identifieri349106 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
    ProteomesiUP000001993: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 899899Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000071929Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi349106.PsycPRwf_0556.

    Structurei

    3D structure databases

    ProteinModelPortaliA5WCX0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini494 – 57784HDUniRule annotationAdd
    BLAST
    Domaini719 – 80486ACT 1UniRule annotationAdd
    BLAST
    Domaini827 – 89973ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 347347UridylyltransferaseAdd
    BLAST
    Regioni348 – 718371Uridylyl-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.

    A5WCX0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFISDPTDSL ITPLPDLTAH SEAQSRNLGI PDWLKQIEAD IATALEKGVD    50
    IRHLVEARAA SIDSLLIELF KLHELTQTDL ALFAVGGYGR GELSPYSDVD 100
    ILILSPDTLS AEISQKVDGF VARLWDVGIE PGIAVRTIED CLQVATDITV 150
    ATNLLEARLL IGNDSLSAIP NNVVQQTWSQ KEFYDAKMAE ARARHLLHNG 200
    TEYNLEPDIK KSPGGLRDIH TIGWITKRYF RITKLYDLVP QDFLTEKEFD 250
    ELMFAEGFLW RIRHHLHHLT GRNENKLLFD YQRDIAERMG YEQSEEDEPN 300
    AAVENFMRDY YRCAMQISTL SEMLTSHYYE TLIEARLPES ERPEKSVLNA 350
    RFNRVGDHIA IAHHHVFAQH PEAILEMFLL MGQHGIKHIR TRTLRALKIA 400
    ARGIDQHYRD NPLHKKLFLD NLKEQNYLFH RLRIMKRYGV LANYMPQFVN 450
    LIGLMQYDLF HRYTVDAHIL LLIRMLHRFT SPKYQDDFAL VGSIYKRIER 500
    KEIIVLAAIF HDIAKGRGGD HSELGERDAI EFCLSHGMSE ADAKLIGWLT 550
    RYHLLMSMTA QKQDISDPEV VTKFANLVGN VTHLNHLYVL TVADMNATNP 600
    QLWNSWRASL MKQLYTQTRR ILRADLDAPT NRQEMIATTR QQALTMLDKV 650
    DNQHMNREEV LALWDELGDE YFLREIPEAI MWHTEAILNH PPIGRASDAN 700
    SEPLIVLREH RELALDAVQI FIYTQDQANL FAVTMAVFDQ MNLDVLDARI 750
    ITATRDFALD SYVLLDRHGT LLTDPESREE LTRRLIDAFK NPETPKLVQK 800
    RLPRRLKNFQ VPTTIDFNYN EASRQHVMSL TTLDQPGLLA RIGQVFLNEG 850
    IEVHAARITT LGERAEDMFY ISDIGDNMLS DAKLERLRTT LIDVLTPSC 899
    Length:899
    Mass (Da):103,339
    Last modified:July 10, 2007 - v1
    Checksum:i52396B5DE7317311
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000713 Genomic DNA. Translation: ABQ93511.1.
    RefSeqiWP_011959838.1. NC_009524.1.
    YP_001279461.1. NC_009524.1.

    Genome annotation databases

    EnsemblBacteriaiABQ93511; ABQ93511; PsycPRwf_0556.
    GeneIDi5204669.
    KEGGiprw:PsycPRwf_0556.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000713 Genomic DNA. Translation: ABQ93511.1 .
    RefSeqi WP_011959838.1. NC_009524.1.
    YP_001279461.1. NC_009524.1.

    3D structure databases

    ProteinModelPortali A5WCX0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349106.PsycPRwf_0556.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ93511 ; ABQ93511 ; PsycPRwf_0556 .
    GeneIDi 5204669.
    KEGGi prw:PsycPRwf_0556.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PPRW349106:GHZF-566-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: PRwf-1.

    Entry informationi

    Entry nameiGLND_PSYWF
    AccessioniPrimary (citable) accession number: A5WCX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 55 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