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Q6LN22

- GLND_PHOPR

UniProt

Q6LN22 - GLND_PHOPR

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Photobacterium profundum (Photobacterium sp. (strain SS9))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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:PBPRA2970
    OrganismiPhotobacterium profundum (Photobacterium sp. (strain SS9))
    Taxonomic identifieri74109 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium
    ProteomesiUP000000593: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 874874Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192750Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi298386.PBPRA2970.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6LN22.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini455 – 588134HDUniRule annotationAdd
    BLAST
    Domaini696 – 77984ACT 1UniRule annotationAdd
    BLAST
    Domaini802 – 87473ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 336336UridylyltransferaseAdd
    BLAST
    Regioni337 – 695359Uridylyl-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.

    Q6LN22-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIDTSTITNP QTLPVEAITQ ENLRNTLEQF AEQQKQQFIQ HRPVTDLVLS    50
    RSTFIDKLLI RLWEHYEVNQ YPDIALVAVG GYGRGELHPL SDVDILILSA 100
    QPLSDETGRI VSKFLTFLWD LRLEVGHSVR TIDDCIEIGN DDLTVATNLT 150
    EARILCGSED VFQCLQERIN AGNFWPSEDF YRAKLEEQKT RHARYHDTTY 200
    NLEPDIKSSP GGLRDIHTLS WVARRHFGAT SLLEMSRFGF LTDAEYRELV 250
    ECQDSLWRIR FALHIELRRY DNRLTFSHQP SVAENLGYTG EGNRGVEMMM 300
    KEFYRTLRRV LELNKMLLQL FDQAILDNGK TVETIQLSDD FQIRGHLIEA 350
    TKPALFQARP ETILDMFLHI AQNGDIEGIA APTLRQLRTA RQRLNVFLVD 400
    IPEAREKFME LVRQPNTLQK AFRLMHRHGV LSAYLPQWSQ IVGQMQFDLF 450
    HVYTVDEHSV RLIKNLNKFN DPENRERHPI CCEVYPRIIK KELLTIAAIF 500
    HDIAKGRGGD HSELGAIEAR KFCIQHGLSR PETNLIAWLV QKHLLMSVTA 550
    QRRDIYDPEV VAEFAKEVRD EERLDYLICL TVADICATNQ ELWNSWKRTL 600
    LAELYYSTQK ALRRGLENTP DVRDRIRHNQ QLSSAILRGK GFAPREIEVL 650
    WKRFKADYFL RHTHKQLAWH AEALLTHDHD KPLILLSKKA TRGGTEVFVY 700
    NKDKAKLFAI VVSELDKKNL SVHDAQIMNS KDGYTLDTFM VLDPSGKTIP 750
    ENRHNTIRRA LVNALTKMKS ERKNKRAPRK LMHFNVKTQV DFLPTKTGKK 800
    TTMELIALDT PGLLARIGAV FAKQKVSLQA AKITTIGERA EDFFILVNEH 850
    GSPLTEEHQQ ALKEALIIKL TPQD 874
    Length:874
    Mass (Da):100,797
    Last modified:July 5, 2004 - v1
    Checksum:iBD18CA770614C067
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR378672 Genomic DNA. Translation: CAG21304.1.
    RefSeqiYP_131106.1. NC_006370.1.

    Genome annotation databases

    EnsemblBacteriaiCAG21304; CAG21304; PBPRA2970.
    GeneIDi3123062.
    KEGGippr:PBPRA2970.
    PATRICi22936978. VBIPhoPro109272_3134.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR378672 Genomic DNA. Translation: CAG21304.1 .
    RefSeqi YP_131106.1. NC_006370.1.

    3D structure databases

    ProteinModelPortali Q6LN22.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 298386.PBPRA2970.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG21304 ; CAG21304 ; PBPRA2970 .
    GeneIDi 3123062.
    KEGGi ppr:PBPRA2970.
    PATRICi 22936978. VBIPhoPro109272_3134.

    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. 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: SS9.

    Entry informationi

    Entry nameiGLND_PHOPR
    AccessioniPrimary (citable) accession number: Q6LN22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 71 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