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A6U5G1

- GLND_SINMW

UniProt

A6U5G1 - GLND_SINMW

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Sinorhizobium medicae (strain WSM419) (Ensifer medicae)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (21 Aug 2007)
      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

    BioCyciSMED366394:GJAL-31-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:Smed_0031
    OrganismiSinorhizobium medicae (strain WSM419) (Ensifer medicae)
    Taxonomic identifieri366394 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
    ProteomesiUP000001108: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 949949Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022354Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi366394.Smed_0031.

    Structurei

    3D structure databases

    ProteinModelPortaliA6U5G1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini494 – 608115HDUniRule annotationAdd
    BLAST
    Domaini734 – 81582ACT 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.
    OMAiLYCLWDM.
    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.

    A6U5G1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARHETSFPE ILDVAALRAR CDFIASAHAE QREPMRRALL AAFKEANIAG    50
    RAKARELLAA DGAGIKCAER ISWLQDQLIT LLHDFVLNQV FDAAKAPETS 100
    RIAVTAVGGY GRGTLAPGSD IDLLFLLPAK KAVWAEPAIE FMLYILWDLG 150
    FKVGHATRTI EDCIRLSRAD MTIRTAILEC RYVCGSVALA SELETRFDHE 200
    IVRNTGPEFI AAKLAERDER HRKAGDTRYL VEPNVKEGKG GLRDLHTLFW 250
    ISKYFYRVKD SADLVKLGVL SRQEYKLFQK AEDFLWAVRC HMHFLTGKAE 300
    ERLSFDIQRE IAEALGYHDH PGLSAVERFM KHYFLVAKDV GDLTRIFCSA 350
    LEDQQAKDAP GISGVISRFR NRVRKIPGTL DFVDDGGRIA LASPDVFKRD 400
    PVNLLRMFHI ADINGLEFHP AALKQVTRSL SLITPHLREN EEANRLFLSI 450
    LTSRRNPELI LRRMNEAAVL GRFIPEFGKI VSMMQFNMYH HYTVDEHLLR 500
    AVDVLSRIER GLEEEAHPLT AMLMPAIEDR EALYVAVLLH DIAKGRPEDH 550
    SVAGAKVARK LCPRFRLSPK QTETVVWLVE EHLTMSMVAQ TRDLNDRKTI 600
    VDFAERVQSL ERLKMLLILT VCDIRAVGPG VWNGWKGQLL RTLYYETELL 650
    LSGGFSELSR KERAKHAADM LEEALADWPK EERQTYVRLH YQPYLLTVAL 700
    DEQVRHAAFI READAAGRTL ATMVRTHDFH AITEITVLSP DHPRLLTVIA 750
    GACAAAGANI VGAQIHTTSD GRALDTILVN REFSVAEDET RRAASIGKLI 800
    EDVLSGRKKL PDVIASRTRS KKRSRAFTVT PEVTISNALS NKFTVIEVEG 850
    LDRTGLLSEV TAVLSDLSLD IASAHITTFG EKVIDTFYVT DLVGSKITSE 900
    NRQMNIAARL KAVLAGEVDE ARERMPSGII APTPVPRASH GSKATKAET 949
    Length:949
    Mass (Da):106,228
    Last modified:August 21, 2007 - v1
    Checksum:iE18E0283457CC20C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000738 Genomic DNA. Translation: ABR58891.1.
    RefSeqiYP_001325726.1. NC_009636.1.

    Genome annotation databases

    EnsemblBacteriaiABR58891; ABR58891; Smed_0031.
    GeneIDi5320858.
    KEGGismd:Smed_0031.
    PATRICi23618827. VBISinMed134228_3085.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000738 Genomic DNA. Translation: ABR58891.1 .
    RefSeqi YP_001325726.1. NC_009636.1.

    3D structure databases

    ProteinModelPortali A6U5G1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 366394.Smed_0031.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR58891 ; ABR58891 ; Smed_0031 .
    GeneIDi 5320858.
    KEGGi smd:Smed_0031.
    PATRICi 23618827. VBISinMed134228_3085.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SMED366394:GJAL-31-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. "Complete sequence of Sinorhizobium medicae WSM419 chromosome."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: WSM419.

    Entry informationi

    Entry nameiGLND_SINMW
    AccessioniPrimary (citable) accession number: A6U5G1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 56 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