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Q8PMJ8

- GLND_XANAC

UniProt

Q8PMJ8 - GLND_XANAC

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Xanthomonas axonopodis pv. citri (strain 306)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (10 Oct 2002)
      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

    BioCyciXAXO190486:GH55-1429-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:XAC1429
    OrganismiXanthomonas axonopodis pv. citri (strain 306)
    Taxonomic identifieri190486 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    ProteomesiUP000000576: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 869869Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192776Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi190486.XAC1429.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8PMJ8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini451 – 570120HDUniRule annotationAdd
    BLAST
    Domaini692 – 77483ACT 1UniRule annotationAdd
    BLAST
    Domaini798 – 86972ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 332332UridylyltransferaseAdd
    BLAST
    Regioni333 – 691359Uridylyl-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.
    HOGENOMiHOG000261778.
    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. 1 hit.
    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.

    Q8PMJ8-1 [UniParc]FASTAAdd to Basket

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    MTDTPAERPD PGVAGDADWA AQARPLLVHV DMRLCKRFDQ GEPIERLVAL    50
    RARAVDQLMR NAWMRCIPAD SGLSLHAVGG YGRGELFPRS DVDVLVLGDT 100
    AAQQQHEQAL ARLFALLWDV GLPISHAVRS PAQCTAAAAD QTVLTALIES 150
    RALVADAQAR AALATAIAPP QVWPPRDFFQ AKREELLARH QRFGDTADNL 200
    EPDIKDGPGG LRDLQTLGWM ALRAFGVKDL EALVGLGHVG FDEAAALRRE 250
    REELARLRFG LHIVANRPEE RLRFDYQKTL AERLGFADDP ESLGVEKMMQ 300
    RFYRSAALIR RISDRLLQRF EEQFDGEATP EPLGGGFSLR RGYLAADTES 350
    WPDGDVLQVF ALFAQWAAHR EVRGLHSLTA RALAEVLRDL PAYEVADATA 400
    RERFMALLRG PRAVETLNRM ARLGVLGQWI PAFASVSGRM QFDLFHVYTV 450
    DQHTLMVLRN IALFAAGRAD EHFSIAHEVW PRLRKPELLL LAGLFHDIAK 500
    GRGGDHSELG AVDARAFCLA HRLSEGDTEL VTWLVEQHLR MSVTAQKQDI 550
    SDPEVIHRFA TLVGTRERLD YLYLLTCADI AGTSPKLWNA WKDRLLADLY 600
    FAARRALREG LEHPPPREER LREARESART LMQAQGHDDV TIDRQFAGMP 650
    DENFLRFRPE QLAWQAASLI EVEIGQTLVK ARRAVPDNDA LEVFVYSPDR 700
    DGLFAAIVAT LDRKGYGIHR ARVLDAPHDA IFDVFEVLPQ ETYADGDPQR 750
    LAATLRQVLA GDLQKVRPAR RAVPRQLRHF RFAPRVEFSE SAGGRRTRIS 800
    LVAPDRPGLL ADVAHVLRMQ HLRVHDARIA TFGERAEDQF QITDEHDRPL 850
    SESARQALRD ALCACLDPV 869
    Length:869
    Mass (Da):97,370
    Last modified:October 10, 2002 - v1
    Checksum:i407F906188598799
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008923 Genomic DNA. Translation: AAM36300.1.
    RefSeqiNP_641764.1. NC_003919.1.
    WP_011050907.1. NC_003919.1.

    Genome annotation databases

    EnsemblBacteriaiAAM36300; AAM36300; XAC1429.
    GeneIDi1155500.
    KEGGixac:XAC1429.
    PATRICi24054857. VBIXanAxo33670_1509.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008923 Genomic DNA. Translation: AAM36300.1 .
    RefSeqi NP_641764.1. NC_003919.1.
    WP_011050907.1. NC_003919.1.

    3D structure databases

    ProteinModelPortali Q8PMJ8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 190486.XAC1429.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM36300 ; AAM36300 ; XAC1429 .
    GeneIDi 1155500.
    KEGGi xac:XAC1429.
    PATRICi 24054857. VBIXanAxo33670_1509.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261778.
    KOi K00990.
    OMAi HHLLMSV.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci XAXO190486:GH55-1429-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. 1 hit.
    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. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
      da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
      , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
      Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 306.

    Entry informationi

    Entry nameiGLND_XANAC
    AccessioniPrimary (citable) accession number: Q8PMJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: October 10, 2002
    Last modified: October 1, 2014
    This is version 85 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