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P23679

- GLND_SALTY

UniProt

P23679 - GLND_SALTY

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 3 (13 Dec 2001)
      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

    BioCyciSENT99287:GCTI-213-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:STM0214
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 890890Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192766Add
    BLAST

    Proteomic databases

    PRIDEiP23679.

    Interactioni

    Protein-protein interaction databases

    STRINGi99287.STM0214.

    Structurei

    3D structure databases

    ProteinModelPortaliP23679.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini468 – 601134HDUniRule annotationAdd
    BLAST
    Domaini709 – 78476ACT 1UniRule annotationAdd
    BLAST
    Domaini816 – 89075ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 349349UridylyltransferaseAdd
    BLAST
    Regioni350 – 708359Uridylyl-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

    HOGENOMiHOG000261778.
    KOiK00990.
    OMAiHHLLMSV.
    OrthoDBiEOG6CCH44.
    PhylomeDBiP23679.

    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.

    P23679-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTLPEQHAN TALPTLPDQP QNPGVWPRAE LTVAGIKARI DIFQHWLGEA    50
    FDSGICAEQL IEARTEFIDQ LLQRLWIEAG FGQIADLALV AVGGYGRGEL 100
    HPLSDIDLLI LSRKKLPDEQ AQKVGELLTL LWDVKLDVGH SVRTLEECLL 150
    EGLSDLTVAT NLIETRLLIG DVALFLALQK HIFSEGFWPS DKFYAAKVEE 200
    QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF GATSLDEMVG 250
    FGFLTPAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN 300
    YSGEGNDPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPV 350
    DDEFQLRGTL IDLRDDTLFI REPQAILRMF YMMVRNSAIT GIYSTTLRHL 400
    RHARRHLSQP LCYIPEARTL FLSMLRHPGA VSRGLLPMHR HSVLWAYMPQ 450
    WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE SFAKEETRQR HPLCVDLWPR 500
    LPHPELILIA ALFHDIAKGR GGDHSVLGAQ DVLTFAELHG LNSRETQLVA 550
    WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTETRLRFL VCLTVADICA 600
    TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL 650
    RMDNIDEAAL HKIWTRCRAN YFVRHSPNQL AWHARHLLQH DLRQPLVLLS 700
    PQATRGGTEI FIWSPDRPYL FAAVCAELDR RNLSVHDAQI FTTRDGMAMD 750
    TFIVLEPDGS PLAADRHDVI RTGLEQTITQ RSWQPPQPRR QPAKLRHFTV 800
    ETEVNFLPTH TDRKSFMELI ALDQPGLLAR VGQIFADLGI SLHGARITTI 850
    GERVEDLFII ATADRRALNN VLQLEVQQRL TAALNPNDKG 890
    Length:890
    Mass (Da):102,264
    Last modified:December 13, 2001 - v3
    Checksum:iB4BF92D1DC4280D0
    GO

    Sequence cautioni

    The sequence CAA39299.1 differs from that shown. Reason: Frameshift at position 88.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011H → D(PubMed:2250660)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL19178.1.
    X55778 Genomic DNA. Translation: CAA39299.1. Frameshift.
    PIRiS12028.
    RefSeqiNP_459219.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL19178; AAL19178; STM0214.
    GeneIDi1251732.
    KEGGistm:STM0214.
    PATRICi32378715. VBISalEnt20916_0227.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL19178.1 .
    X55778 Genomic DNA. Translation: CAA39299.1 . Frameshift.
    PIRi S12028.
    RefSeqi NP_459219.1. NC_003197.1.

    3D structure databases

    ProteinModelPortali P23679.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM0214.

    Proteomic databases

    PRIDEi P23679.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL19178 ; AAL19178 ; STM0214 .
    GeneIDi 1251732.
    KEGGi stm:STM0214.
    PATRICi 32378715. VBISalEnt20916_0227.

    Phylogenomic databases

    HOGENOMi HOG000261778.
    KOi K00990.
    OMAi HHLLMSV.
    OrthoDBi EOG6CCH44.
    PhylomeDBi P23679.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-213-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    2. "Cloning and nucleotide sequence of the Salmonella typhimurium pepM gene."
      Movva N.R., Semon D., Meyer C., Kawashima E., Wingfield P., Miller J.L., Miller C.G.
      Mol. Gen. Genet. 223:345-348(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
      Strain: LT2.
    3. Robison K.
      Unpublished observations (OCT-1992)
      Cited for: IDENTIFICATION OF PROTEIN.

    Entry informationi

    Entry nameiGLND_SALTY
    AccessioniPrimary (citable) accession number: P23679
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: December 13, 2001
    Last modified: October 1, 2014
    This is version 112 of the entry and version 3 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