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Q9JZB4

- GLND_NEIMB

UniProt

Q9JZB4 - GLND_NEIMB

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Neisseria meningitidis serogroup B (strain MC58)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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

    BioCyciNMEN122586:GHGG-1240-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:NMB1203
    OrganismiNeisseria meningitidis serogroup B (strain MC58)
    Taxonomic identifieri122586 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000000425: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192748Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi122586.NMB1203.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JZB4.
    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.
    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.
    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.

    Q9JZB4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPANLSSALE TFKQQRDAAE AHYLKANRVS VFFREYTAAV ETLLAALWAE    50
    YFQNSALCLM AVGGFGRGEL YPCSDVDLAV VSPAPLSDGI QEQIARFVQT 100
    LWDCKLMPSV KSGSVDELCE SVRNDITGDT AFLEARFLFG NRQTVDKLAE 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 QNPENRRRFA GFFRNGNGLT 400
    QTLRFLNLYG VLGRYLPAWE KIIGLLQHDL FHIYPVDDHI LTVVRNVRRL 450
    ALDMHSHELP YASALMQSFE KQDILYLAAF FHDIAKGRGG DHAIQGIADA 500
    RQFAADHFLT GEESDLLAWL VENHLLMSAV AQKEDIQDPS VLDAFCKRVQ 550
    THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RYLTGNGGNP 600
    HTLFGRRRQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA 650
    NLVHDFETPI VRSRILPKSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL 700
    AARAFITEHD YILDTFIVQI PSQHAPEDYP DIQSALEAEL NSFIHGHTVA 750
    ETQSRSRRIS RRSRYMPIAP SITITPEEDY PDWYSVEITA VNRPFLLADM 800
    AEVFFAHNVS LRYAKISTLD ERAEDSFTVF SPDLKNPKIQ SSLKQTLLEQ 850
    LS 852
    Length:852
    Mass (Da):97,008
    Last modified:October 1, 2000 - v1
    Checksum:i1F377E3C95355F1B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002098 Genomic DNA. Translation: AAF41585.1.
    PIRiB81110.
    RefSeqiNP_274228.1. NC_003112.2.

    Genome annotation databases

    EnsemblBacteriaiAAF41585; AAF41585; NMB1203.
    GeneIDi903625.
    KEGGinme:NMB1203.
    PATRICi20357995. VBINeiMen85645_1510.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002098 Genomic DNA. Translation: AAF41585.1 .
    PIRi B81110.
    RefSeqi NP_274228.1. NC_003112.2.

    3D structure databases

    ProteinModelPortali Q9JZB4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 122586.NMB1203.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF41585 ; AAF41585 ; NMB1203 .
    GeneIDi 903625.
    KEGGi nme:NMB1203.
    PATRICi 20357995. VBINeiMen85645_1510.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci NMEN122586:GHGG-1240-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MC58.

    Entry informationi

    Entry nameiGLND_NEIMB
    AccessioniPrimary (citable) accession number: Q9JZB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 88 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3