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P56884

- GLND_RHIME

UniProt

P56884 - GLND_RHIME

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (30 May 2000)
      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.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 fixation Source: UniProtKB-HAMAP
    2. regulation of nitrogen utilization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Nitrogen fixation

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciSMEL266834:GJF6-407-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:R00396
    ORF Names:SMc01124
    OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
    Taxonomic identifieri266834 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
    ProteomesiUP000001976: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 949949Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192760Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi266834.SMc01124.

    Structurei

    3D structure databases

    ProteinModelPortaliP56884.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini494 – 608115HDUniRule annotationAdd
    BLAST
    Domaini734 – 81683ACT 1UniRule annotationAdd
    BLAST
    Domaini845 – 92682ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 377377UridylyltransferaseAdd
    BLAST
    Regioni378 – 733356Uridylyl-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.
    HOGENOMiHOG000261779.
    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.

    P56884-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARHETSFPE ILDVAALRAR CDFIASAHAE QREPMRRALL AAFKEANVAG    50
    RAKARELLAA DGAGIKCAER ISWLQDQLIT LLHDFVLNQV FDAAKAPEAS 100
    RIAVTAVGGY GRGTLAPGSD IDLLFLLPAK KAVWAEPAIE FMLYILWDLG 150
    FKVGHATRTI EECIRLSRAD MTIRTAILEC RYVCGSAALA NELETRFDHE 200
    IVRNTGPEFI AAKLAERDER HRKAGDTRYL VEPNVKEGKG GLRDLHTLFW 250
    ISKYFYRVKD SADLVKLGVL SKQEYKLFQK AEDFLWAVRC HMHFLTGKAE 300
    ERLSFDIQRE IAEALGYHDH PGLSAVERFM KHYFLVAKDV GDLTRIFCSA 350
    LEDQQAKDTP GITGVISRFR NRVRKIAGTL DFVDDGGRIA LAGTDVFKRD 400
    PVNLMRLFHI ADINGLEFHP AALKQVTRSL GLITPHLREN EEANRLFLSI 450
    LTSRRNPELI LRRMNEAGVL GRFIPEFGKI VSMMQFNMYH HYTVDEHLLR 500
    SVDVLSRIER GLEEEAHPLT AMLMPGIEDR EALYVAVLLH DIAKGRPEDH 550
    SVAGAKVARK LCPRFRLTPK QTEMVVWLVE EHLTMSMVAQ TRDLNDRKTI 600
    VDFAERVQSL ERLKMLLILT VCDIRAVGPG VWNGWKGQLL RTLYYETELL 650
    LSGGFSELSR KERAKHAAHM LEEALADWPK KERQAYVRLH YQPYLLTVAL 700
    EEQVRHAGFI READRAGRTL ATMVRTHDFH AITEITVLSP DHPRLLTVIA 750
    GACAAAGANI VGAQIHTTSD GRALDTILVN REFSVAEDET RRAASIGKLI 800
    EDVLSGRKRL PEVIASRTRV KKRSRAFTVT PEVTISNTLS NKFTVIEVEG 850
    LDRTGLLSEV TAVLSDLSLD IASAHITTFG EKVIDTFYVT DLVGSKITSE 900
    NRQMNIAARL KAVLAGEVDE ARERMPSGII APTPVSRVPH GSKTTKAET 949
    Length:949
    Mass (Da):106,382
    Last modified:May 30, 2000 - v1
    Checksum:iEF549C1B0D8540A0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF227730 Genomic DNA. Translation: AAF37852.1.
    AL591688 Genomic DNA. Translation: CAC41833.1.
    RefSeqiNP_384502.1. NC_003047.1.
    WP_003527696.1. NC_003047.1.

    Genome annotation databases

    EnsemblBacteriaiCAC41833; CAC41833; SMc01124.
    GeneIDi1232030.
    KEGGisme:SMc01124.
    PATRICi23629999. VBISinMel96828_1769.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF227730 Genomic DNA. Translation: AAF37852.1 .
    AL591688 Genomic DNA. Translation: CAC41833.1 .
    RefSeqi NP_384502.1. NC_003047.1.
    WP_003527696.1. NC_003047.1.

    3D structure databases

    ProteinModelPortali P56884.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266834.SMc01124.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC41833 ; CAC41833 ; SMc01124 .
    GeneIDi 1232030.
    KEGGi sme:SMc01124.
    PATRICi 23629999. VBISinMel96828_1769.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261779.
    KOi K00990.
    OMAi HHLLMSV.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci SMEL266834:GJF6-407-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. 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. "glnD and mviN are genes of an essential operon in Sinorhizobium meliloti."
      Rudnick P.A., Arcondeguy T., Kennedy C.K., Kahn D.
      J. Bacteriol. 183:2682-2685(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1021.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1021.

    Entry informationi

    Entry nameiGLND_RHIME
    AccessioniPrimary (citable) accession number: P56884
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 93 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