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B0KS97

- GLND_PSEPG

UniProt

B0KS97 - GLND_PSEPG

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pseudomonas putida (strain GB-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (18 Mar 2008)
      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

    BioCyciPPUT76869:GIXB-1174-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:PputGB1_1144
    OrganismiPseudomonas putida (strain GB-1)
    Taxonomic identifieri76869 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002157: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000078808Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi76869.PputGB1_1144.

    Structurei

    3D structure databases

    ProteinModelPortaliB0KS97.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini481 – 590110HDUniRule annotationAdd
    BLAST
    Domaini706 – 78479ACT 1UniRule annotationAdd
    BLAST
    Domaini816 – 90085ACT 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.

    B0KS97-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPQVDPELFD RGQFQAELAL KASPIAAFKK AIRLAGEVLD KRFRAGSEIR    50
    PLIEARAWLV DNILQQAWNQ FDWGDQSGIA LVAVGGYGRG ELHPHSDIDL 100
    LILLGAAEHE QYRDAIERFL TLLWDIGLEV GQSVRTVDEC AEQARADLTV 150
    ITNLMESRTI CGPEALRQRM LEVTSTAHMW PSKEFFLAKR AELKARHHKY 200
    NDTEYNLEPN VKGSPGGLRD IQTVLWVARR QYGTLNLHAL AGEGFLLESE 250
    NELLASSQDF LWKVRYALHM LAGRAEDRLL FDHQRSLATL LGYGDDNPKR 300
    AIEQFMQQYY RVVMSISQLC DLIVQHFEEV ILADEESGST QPLNARFRLH 350
    DGYIEAANPN VFKRTPFAML EIFVLMAQRP EIKGVRADTV RLLREHRHLI 400
    DDTFRTDIRN TSLFIELFKC EIGIHRNLRR MNRYGILGRY LPEFGLIVGQ 450
    MQHDLFHIYT VDAHTLNLIK HLRKLQYTPV SEKFPLASKL MGRLPKPELI 500
    YLAGLYHDIG KGRQGDHSEI GAVDAQKFCE RHQLPAWDSR LIVWLVQNHL 550
    VMSTTAQRKD LSDPQVINDF ALHVGDETRL DYLYVLTVAD INATNPSLWN 600
    SWRASLLRQL YTETKRALRR GLENPLDREE QIRQTQSSAL DILVREGTDP 650
    DDVEQLWSQL GDDYFLKHNA ADVAWHTDAI LQQPADGGPL VLIKETTQRE 700
    FEGGTQIFIY APDQHDFFAV TVAAMSQLNL NIHDARIITS SSQFTLDTYI 750
    VLDNDGGSIG DNPQRVKQIR DGLTEALRNP EDYPTIIQRR VPRQLKHFDF 800
    PPQVTILNDA QRPVTILEIT APDRPGLLAR LGRIFLEFDL SLQNAKIATL 850
    GERVEDVFFI TDADNQPLSD PQLCSRLQEA IVQQLQAGQG SDTSPTRVTF 900
    Length:900
    Mass (Da):102,573
    Last modified:March 18, 2008 - v1
    Checksum:i7650D665F9A853D7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000926 Genomic DNA. Translation: ABY97052.1.
    RefSeqiYP_001667388.1. NC_010322.1.

    Genome annotation databases

    EnsemblBacteriaiABY97052; ABY97052; PputGB1_1144.
    GeneIDi5868903.
    KEGGippg:PputGB1_1144.
    PATRICi19929261. VBIPsePut76638_1150.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000926 Genomic DNA. Translation: ABY97052.1 .
    RefSeqi YP_001667388.1. NC_010322.1.

    3D structure databases

    ProteinModelPortali B0KS97.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 76869.PputGB1_1144.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABY97052 ; ABY97052 ; PputGB1_1144 .
    GeneIDi 5868903.
    KEGGi ppg:PputGB1_1144.
    PATRICi 19929261. VBIPsePut76638_1150.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PPUT76869:GIXB-1174-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: GB-1.

    Entry informationi

    Entry nameiGLND_PSEPG
    AccessioniPrimary (citable) accession number: B0KS97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 47 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