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Q4KHH8

- GLND_PSEF5

UniProt

Q4KHH8 - GLND_PSEF5

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (02 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

    BioCyciPFLU220664:GIX8-1178-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:PFL_1174
    OrganismiPseudomonas fluorescens (strain Pf-5 / ATCC BAA-477)
    Taxonomic identifieri220664 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000008540: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192753Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi220664.PFL_1174.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4KHH8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini481 – 57696HDUniRule annotationAdd
    BLAST
    Domaini706 – 78984ACT 1UniRule annotationAdd
    BLAST
    Domaini816 – 89580ACT 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.

    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.

    Q4KHH8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPQVDPELFD RGQFQAELAL KASPIAAFKK AIRQAREVLD TRFRSGREIR    50
    RLIEDRAWFI DNILQKAWDQ FSWSEDADIA LVAVGGYGRG ELHPYSDIDL 100
    LILLDSADHE IFRDSIERFL TLLWDIGLEV GQSVRSVDEC AEQARADLTV 150
    ITNLMESRTI AGPEHLRQRM LQVTSTEHMW PSKDFFLAKR AEQKARHHKY 200
    NDTEYNLEPN VKGSPGGLRD IQTILWVARR QYGTLNLRAL AGEGFLVESE 250
    NALLASSQEF LWKVRYALHM LAGRAEDRLL LDHQRSIATL LGFEGEDAKQ 300
    SIESFMQQYY RVVMSIAQLS DLIIQHFEEV ILAPEDEAPP QPINARFQLH 350
    DGYIEAINDN VFKRTPFAML EIFVLMAQHP EIKGVRADTI RLLREHRHLI 400
    DDDFRHDIRN TSLFIELFKC EIGIHRNLRR MNRYGILGRY LPEFGFIVGQ 450
    MQHDLFHIYT VDAHTLNLIK HLRKMQYTPI SEKFPLASKL MGKLPKPELI 500
    YLAGLYHDIG KGRHGDHSEI GAVDAEAFCV RHQLPQWDTR LIVWLVQNHL 550
    VMSTTAQRKD LSDPQVIHDF AQIVVDQTRL DYLYVLTVAD IYATNPTLWN 600
    SWRASLLRQL YTETKRALRR GLENPVDREE QIRQTQSAAL DILVRNGTDP 650
    DEVEQLWSQL GDDYFLRHTA GDVAWHSDAI LQQPADGGPL VLIKEITQRE 700
    FEGGTQIFIY APDQHDFFAV TVAAMDQLNL NIHDARIITS SSQFTLDTYI 750
    VLDNDGESIG NNPQRVEQIR KGLTDALRNP DDYPTIIQRR VPRQLKHFAF 800
    APEVTIHNDA QRPVTVLELS APDRPGLLAR IGKIFLEFDL SLQNAKIATL 850
    GERVEDVFFI TDAHNQPLSD PQLCSRLQDA IVEQLSVSHE PTIEMTRLSI 900
    Length:900
    Mass (Da):103,314
    Last modified:August 2, 2005 - v1
    Checksum:i40F0D6C35069651E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000076 Genomic DNA. Translation: AAY90461.1.
    RefSeqiYP_258305.1. NC_004129.6.

    Genome annotation databases

    EnsemblBacteriaiAAY90461; AAY90461; PFL_1174.
    GeneIDi3478991.
    KEGGipfl:PFL_1174.
    PATRICi19871555. VBIPseFlu72549_1206.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000076 Genomic DNA. Translation: AAY90461.1 .
    RefSeqi YP_258305.1. NC_004129.6.

    3D structure databases

    ProteinModelPortali Q4KHH8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 220664.PFL_1174.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAY90461 ; AAY90461 ; PFL_1174 .
    GeneIDi 3478991.
    KEGGi pfl:PFL_1174.
    PATRICi 19871555. VBIPseFlu72549_1206.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PFLU220664:GIX8-1178-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: Pf-5 / ATCC BAA-477.

    Entry informationi

    Entry nameiGLND_PSEF5
    AccessioniPrimary (citable) accession number: Q4KHH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: August 2, 2005
    Last modified: October 1, 2014
    This is version 66 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