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Q7N8P9

- GLND_PHOLL

UniProt

Q7N8P9 - GLND_PHOLL

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Photorhabdus luminescens subsp. laumondii (strain TT01)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      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:plu0670
    OrganismiPhotorhabdus luminescens subsp. laumondii (strain TT01)
    Taxonomic identifieri243265 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus
    ProteomesiUP000002514: Chromosome

    Organism-specific databases

    GenoListiplu0670.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 882882Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192751Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243265.plu0670.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7N8P9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini462 – 595134HDUniRule annotationAdd
    BLAST
    Domaini701 – 77878ACT 1UniRule annotationAdd
    BLAST
    Domaini808 – 88275ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 343343UridylyltransferaseAdd
    BLAST
    Regioni344 – 700357Uridylyl-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. 2 hits.
    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.

    Q7N8P9-1 [UniParc]FASTAAdd to Basket

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    MSADIATIQA PIPPLSPADF SSEDLRYPVL KQHLEEFQLW LEHAFKAGIS    50
    AEALISARSD YIDQLLQQLW YAYRFDKISS LSLIAVGGYG RRELHPLSDI 100
    DVLILSEQPL TPPQAQNVGQ FITLLWDIRL EVGHSVRTLE ECLLEGLSDL 150
    TIATNLIESR LICGDSSIFL RLQRHTFSDG FWPSTEFFDA KIVEQHERHQ 200
    RYHSTSYNLE PDIKSSPGGL RDIHTLLWVA RRHFGATSID EMVDFGFLTA 250
    EERNELNECQ SFLWRIRFAL HLVVNRYDNR LLFDRQFSIA QLLGYHGERN 300
    QPVERMMKDF YRMTRRVSEL NNMLLQLFDE AILALETNEK SRSLDSEFQL 350
    RGQLIDLIDE TLFIKEPAAI MRMFYRMAEH EEVQGIYSTT LRHLRYARRN 400
    LSQPLCELPE ARQIFMDILR HPRAVESAFV PMHRHSVLGA YTPLWGNIVG 450
    QMQFDLFHAY TVDEHTIRVL RKLESFANEN NRPAHPLCVE LYPRLPQPEL 500
    LHLAALFHDI AKGRTGDHSE LGADDALAFS LKHGLNSREA DLVAWLVRHH 550
    LLMSVTAQRR DIQDPEIIKQ FTHQILNETR LRYLICLTVA DICATNVNLW 600
    NSWKQSLLRE LYFSTENQLR QGNTPDFRER IRHNRFQALA LLRQDNINEQ 650
    KLHQLWSRCH ADYFLRHTPK QLAWHAHHLV QHDSQESLIL ISTKPTRGGT 700
    EIFIWSVDRP SLFAAVVGEL DRRNLSVHHA QIFTNRDGMT MDTFVVLEPN 750
    GHPLASDRHE IIRNALLQVV LAPHTKTPKT RKLPTKLRHF NVPTKVTFLP 800
    THNERRTYME LFALDQPGLL ARVGNIFAEM GVSLHGAHIT TIGERVEDFF 850
    VLADKDHKAL NKKVREELSE RLTATLNPKD KI 882
    Length:882
    Mass (Da):102,232
    Last modified:December 15, 2003 - v1
    Checksum:i12FEA798C315CBCD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571861 Genomic DNA. Translation: CAE12965.1.
    RefSeqiNP_928015.1. NC_005126.1.
    WP_011145046.1. NC_005126.1.

    Genome annotation databases

    EnsemblBacteriaiCAE12965; CAE12965; plu0670.
    GeneIDi2800627.
    KEGGiplu:plu0670.
    PATRICi20504919. VBIPhoLum48522_0738.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571861 Genomic DNA. Translation: CAE12965.1 .
    RefSeqi NP_928015.1. NC_005126.1.
    WP_011145046.1. NC_005126.1.

    3D structure databases

    ProteinModelPortali Q7N8P9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243265.plu0670.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE12965 ; CAE12965 ; plu0670 .
    GeneIDi 2800627.
    KEGGi plu:plu0670.
    PATRICi 20504919. VBIPhoLum48522_0738.

    Organism-specific databases

    GenoListi plu0670.

    Phylogenomic databases

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

    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. 2 hits.
    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: TT01.

    Entry informationi

    Entry nameiGLND_PHOLL
    AccessioniPrimary (citable) accession number: Q7N8P9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 74 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