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P41393

- GLND_KLEOX

UniProt

P41393 - GLND_KLEOX

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Klebsiella oxytoca
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 fixation and metabolism Probable.1 Publication

    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 fixation Source: UniProtKB-KW
    2. regulation of nitrogen utilization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Nitrogen fixation

    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
    OrganismiKlebsiella oxytoca
    Taxonomic identifieri571 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are unable to uridylylate PII and are altered in adenylation/deadenylation of glutamine synthetase.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 887887Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192739Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP41393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini465 – 598134HDUniRule annotationAdd
    BLAST
    Domaini706 – 78681ACT 1UniRule annotationAdd
    BLAST
    Domaini813 – 88775ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 346346UridylyltransferaseAdd
    BLAST
    Regioni347 – 705359Uridylyl-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

    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.

    P41393-1 [UniParc]FASTAAdd to Basket

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    MSNSLSNTVP PDLSAQPENP GEWPKSDFNC ATIKALIDAF QRWLGEAFDS    50
    GIAAERLIEA RTEFIDQLLQ RLWVEYGFGS INDIALVAVG GYGRGELHPL 100
    SDIDLLILSR KKLPDEQAQK VGERLALLWD IKLEVGHSVR TLEECLLEGL 150
    SDLSVATNLI ESRLLIGDVA LFLELQKHIF SDGFWPSEKF FAAKVEEQND 200
    RHQRYHGTSY NLEPDVKSSP GGLRDIHTLQ WIARRHFGAT SLDEMVGFGF 250
    LTEAERNELN ECLHQLWRIR FALHLELNRY DNRLLFDRQF SVARRLRYEG 300
    ESNQPIEHMM KDFFRVTRRV SELNQMLIQL FEEAILALTE DEKPRPIDDD 350
    FQLRGTLIDL RDDTLFIREP QAILRMFYTM VRNSSITGIY STTVRHLRHA 400
    RRHLTQPLCY IPEARTLFLS MLRHQGGLSR GLLPMHRHSV LWAYMPQWSH 450
    IVGQMQFDLF HAYTVDEHTI RVLLKLESFA KEETRSRHPL WLELWPRLTH 500
    PELILIAALF HDIAKGAGGD HSILGAQDVL KFAELHGLNC AQTQLVAWLV 550
    RHQLLMSVTA QRRDIQDPEV IKQFAEEVQT ENRLHYLVCL TVADICATNE 600
    NLWNSWKQSL LRELYFATEK QLRRGMQNTP DMRERVRHHQ LQALALLRME 650
    NINEQALHQI WNRCRANYFV RHTPNQLAWH ARNLLKHDLS KPMILLSSHA 700
    TRGGTEIFIW SPDRPYLFAA VSAELDRRNL SVHDAQIFTT RDGMAMDTFI 750
    VLEPDGSPLS ADRTQMIRVG LEQTLSQRSW QPPAPRRQAA KLRHFSVPTE 800
    VNFLPTHTDR KSFLELIALD QPGLLARVGQ VFADLGISLH GARITTIGER 850
    VEDLFIIATA DRRALNNELQ QEVQQRLTEA LNPNDKG 887
    Length:887
    Mass (Da):102,344
    Last modified:November 1, 1995 - v1
    Checksum:i73782E94DA434CAC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78685 Genomic DNA. Translation: CAA55353.1.
    PIRiS54756. S43196.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78685 Genomic DNA. Translation: CAA55353.1 .
    PIRi S54756. S43196.

    3D structure databases

    ProteinModelPortali P41393.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "The role of uridylyltransferase in the control of Klebsiella pneumoniae nif gene regulation."
      Edwards R.A., Merrick M.J.
      Mol. Gen. Genet. 247:189-198(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE.
      Strain: M5a1.

    Entry informationi

    Entry nameiGLND_KLEOX
    AccessioniPrimary (citable) accession number: P41393
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 75 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

    Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3