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A5U6S3

- GLND_MYCTA

UniProt

A5U6S3 - GLND_MYCTA

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (10 Jul 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 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

    BioCyciMTUB419947:GJ8N-3043-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:MRA_2943
    OrganismiMycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
    Taxonomic identifieri419947 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001988: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 808808Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022346Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi419947.MRA_2943.

    Structurei

    3D structure databases

    ProteinModelPortaliA5U6S3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini431 – 536106HDUniRule annotationAdd
    BLAST
    Domaini610 – 68677ACT 1UniRule annotationAdd
    BLAST
    Domaini730 – 80576ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 315315UridylyltransferaseAdd
    BLAST
    Regioni316 – 609294Uridylyl-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.
    HOGENOMiHOG000021840.
    KOiK00990.
    OMAiRRPIDEG.
    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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF01842. ACT. 1 hit.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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.

    A5U6S3-1 [UniParc]FASTAAdd to Basket

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    MEAESPCAAS DLAVARRELL SGNHRELDPV GLRQTWLDLH ESWLIDKADE    50
    IGIADASGFA IVGVGGLGRR ELLPYSDLDV LLLHDGKPAD ILRPVADRLW 100
    YPLWDANIRL DHSVRTVSEA LTIANSDLMA ALGMLEARHI AGDQQLSFAL 150
    IDGVRRQWRN GIRSRMGELV EMTYARWRRC GRIAQRAEPD LKLGRGGLRD 200
    VQLLDALALA QLIDRHGIGH TDLPAGSLDG AYRTLLDVRT ELHRVSGRGR 250
    DHLLAQFADE ISAALGFGDR FDLARTLSSA GRTIGYHAEA GLRTAANALP 300
    RRGISALVRR PKRRPLDEGV VEYAGEIVLA RDAEPEHDPG LVLRVAAASA 350
    DTGLPIGAAT LSRLAASVPD LPTPWPQEAL DDLLVVLSAG PTTVATIEAL 400
    DRTGLWGRLL PEWEPIRDLP PRDVAHKWTV DRHVVETAVH AAPLATRVAR 450
    PDLLALGALL HDIGKGRGTD HSVLGAELVI PVCTRLGLSP PDVRTLSKLV 500
    RHHLLLPITA TRRDLNDPKT IEAVSEALGG DPQLLEVLHA LSEADSKATG 550
    PGVWSDWKAS LVDDLVRRCR MVMAGESLPQ AEPTAPHYLS LAADHGVHVE 600
    ISPRDGERID AVIVAPDERG LVSKAAAVLA LNSLRVHSAS VNVHQGVAIT 650
    EFVVSPLFGS PPAAELVRQQ FVGALNGDVD VLGMLQKRDS DAASLVSARA 700
    GDVQAGVPVT RTAAPPRILW LDTAAPAKLI LEVRAMDRAG LLALLAGALE 750
    GAGAGIVWAK VNTFGSTAAD VFCVTVPAEL DARAAVEQHL LEVLGASVDV 800
    VVDEPVGD 808
    Length:808
    Mass (Da):86,438
    Last modified:July 10, 2007 - v1
    Checksum:i9B1F14D01C29F0B0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000611 Genomic DNA. Translation: ABQ74723.1.
    RefSeqiYP_001284285.1. NC_009525.1.

    Genome annotation databases

    EnsemblBacteriaiABQ74723; ABQ74723; MRA_2943.
    GeneIDi5215487.
    KEGGimra:MRA_2943.
    PATRICi18146209. VBIMycTub106795_3293.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000611 Genomic DNA. Translation: ABQ74723.1 .
    RefSeqi YP_001284285.1. NC_009525.1.

    3D structure databases

    ProteinModelPortali A5U6S3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 419947.MRA_2943.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ74723 ; ABQ74723 ; MRA_2943 .
    GeneIDi 5215487.
    KEGGi mra:MRA_2943.
    PATRICi 18146209. VBIMycTub106795_3293.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000021840.
    KOi K00990.
    OMAi RRPIDEG.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci MTUB419947:GJ8N-3043-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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view ]
    Pfami PF01842. ACT. 1 hit.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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 genomic sequence of Mycobacterium tuberculosis strain H37Ra, a non-pathogenic variant closely related to the well-characterized pathogenic strain H37Rv."
      Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25177 / H37Ra.

    Entry informationi

    Entry nameiGLND_MYCTA
    AccessioniPrimary (citable) accession number: A5U6S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 59 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