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A9LZ86

- GLND_NEIM0

UniProt

A9LZ86 - GLND_NEIM0

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Neisseria meningitidis serogroup C (strain 053442)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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

    BioCyciNMEN374833:GJ7Z-1084-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:NMCC_1086
    OrganismiNeisseria meningitidis serogroup C (strain 053442)
    Taxonomic identifieri374833 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000001177: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000078806Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi374833.NMCC_1086.

    Structurei

    3D structure databases

    ProteinModelPortaliA9LZ86.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini437 – 539103HDUniRule annotationAdd
    BLAST
    Domaini673 – 75785ACT 1UniRule annotationAdd
    BLAST
    Domaini785 – 85268ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 318318UridylyltransferaseAdd
    BLAST
    Regioni319 – 672354Uridylyl-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.
    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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF08335. 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.

    A9LZ86-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPANLSSALE TFKRQRDAAE AHYLKANRVS VFFREYTAAV ETLLAALWVE    50
    HFQNSALCLM AVGGFGRGEL YPCSDVDLAV VSPAPLSDGI QEQIARFVQT 100
    LWDCKLMPSV KSGSVGELCE SVRDDITGDT AFLEARFLFG NRQTADELAK 150
    KMNAQRNVAA FVEAKLVEME HRHAKSQGSG AVLEPNIKSC PGGLRDIHTL 200
    LWIAKAQGLA TDLPDLLKQR ILTRAEAGML SHGYRRLAHI RIHLHLNAKR 250
    AEDRLLFDLQ PQVAESMGYE GLNLRRQSEE LMRVFYRAIK TVKQLGGILT 300
    PMLQSRVSST PLRVTLRIDD DYIQVNNQIA ARHTDIFFRR PEHIFKIVEI 350
    MQQRNDITAL EPQTLRAWWG ATRKINRSFY QNSENRHRFA GFFRNGNGLT 400
    QTLRFLNLYG VLGRYLPAWE KIVGLLQHDL FHIYPVDDHI LTVVRNVRRL 450
    ALDMHSHELP YASALMQSFE KQDILYLAAF FHDIAKGRGG DHAIQGIADA 500
    RQFAADHFLT EEESDLLAWL VENHLLMSTV AQKEDIQDPS VLDAFCKRVQ 550
    THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RYLTGNGGNP 600
    HTLFGRRRQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA 650
    NLVHDFETPI VRSRILPQSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL 700
    AARAFITEHD YILDTFIVQI PSQHAPEDYP DIQSALEAEL NSFIHGHTVA 750
    EISSHSRRIS RRSRYMPIAP SITITPEEDY PDWYSVEITA VNRPFLLADM 800
    AEVFFAHNVS LRYAKISTLD ERAEDSFTVF SPDLNNPKIQ SSLKQTLLEQ 850
    LS 852
    Length:852
    Mass (Da):96,950
    Last modified:February 5, 2008 - v1
    Checksum:i6E3897F76ABFCCE0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000381 Genomic DNA. Translation: ABX73263.1.
    RefSeqiYP_001599219.1. NC_010120.1.

    Genome annotation databases

    EnsemblBacteriaiABX73263; ABX73263; NMCC_1086.
    GeneIDi5796239.
    KEGGinmn:NMCC_1086.
    PATRICi20346794. VBINeiMen117761_1313.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000381 Genomic DNA. Translation: ABX73263.1 .
    RefSeqi YP_001599219.1. NC_010120.1.

    3D structure databases

    ProteinModelPortali A9LZ86.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 374833.NMCC_1086.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX73263 ; ABX73263 ; NMCC_1086 .
    GeneIDi 5796239.
    KEGGi nmn:NMCC_1086.
    PATRICi 20346794. VBINeiMen117761_1313.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci NMEN374833:GJ7Z-1084-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 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. "Characterization of ST-4821 complex, a unique Neisseria meningitidis clone."
      Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z., Liang X., Xu J., Jin Q.
      Genomics 91:78-87(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 053442.

    Entry informationi

    Entry nameiGLND_NEIM0
    AccessioniPrimary (citable) accession number: A9LZ86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 50 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