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Q2Y5Q1

- GLND_NITMU

UniProt

Q2Y5Q1 - GLND_NITMU

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      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

    BioCyciNMUL323848:GKEC-2679-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:Nmul_A2633
    OrganismiNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849)
    Taxonomic identifieri323848 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira
    ProteomesiUP000002718: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 887887Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231684Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi323848.Nmul_A2633.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2Y5Q1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini448 – 555108HDUniRule annotationAdd
    BLAST
    Domaini687 – 77286ACT 1UniRule annotationAdd
    BLAST
    Domaini796 – 87176ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 329329UridylyltransferaseAdd
    BLAST
    Regioni330 – 686357Uridylyl-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.

    Q2Y5Q1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGLNAKPFS HEAVRQKLLS GRESLQRRYH QNRNGAALLR DHSRLVDGIL    50
    RQVWHEMNMP GSTALLAVGG YGRRQLFPYS DIDLVVLLPD KGDAAEAMDN 100
    ELGTRLEHWV GLLWDIGLDI GHSVRTVKEC GEEAANDITV QTSLLEARLL 150
    GGNSDLFDRF LQVMETMLAP RKFFVDKQLE QQQRHKRYQD APYKLEPNIK 200
    ESPGGLRDLQ NVLWISRAAG FGKTWSELAK KGFIIRREAR LIQRQQTVLQ 250
    DLRIRLHYLG GRREDRLLFD YQNPLAEELG IAAKPPRRPG EMLMQRYYRA 300
    ARSVTQVNTI LLLTLHAEIF PDEEAVTTII NERFQKRGDL LEICEEDIFE 350
    RDPGAILESV LLLQQNPDLK GRSFATLRAM WRSAPLITAS FRREPRHCAM 400
    FMEILRQPRG LTRELRLMNR YGILGRYIPA FGRIIGQMQH DLFHVYTVDE 450
    HILMVVRNLR RFMAPEFAYE YPLCSRLINE FERPELLYLA GLFHDIAKGR 500
    QGDHSLLGKV DARRFCERHR MPAEDTELVV WLVENHLHMS ATAQKKDIAD 550
    AEVIADFAAS MRDERHLIAL YLLTVSDIRG TSPKVWNAWK GKLLEDLFHR 600
    TRQYLCGETA LTDISLENRK NKVLQLLHPD DAAMRAYERF WSGLDSSYLM 650
    MHDPREIAWH TQHLSQRMKS PAPIVKTRAA ETGAGVEVLV YTADQKDLFA 700
    RICSFFDGID YNIVQAKIHT TREGYALDSF LVLDPFNVAN HDPREFQFIE 750
    QELTQQLEQQ ALMATPVKGR LSRHLRHFPI TPQVSIEPDD SGAYYVLSIT 800
    AGDQSGLLSR IAQVLVRFGL NVHSARINTL GERAEDTFLV TGSILSNSRS 850
    VIQLEANLIK VLHTSPQPET PGKAPGKPSA GDRIIPR 887
    Length:887
    Mass (Da):101,510
    Last modified:December 20, 2005 - v1
    Checksum:iE65E0364AA37D84B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000103 Genomic DNA. Translation: ABB75920.1.
    RefSeqiYP_413312.1. NC_007614.1.

    Genome annotation databases

    EnsemblBacteriaiABB75920; ABB75920; Nmul_A2633.
    GeneIDi3786336.
    KEGGinmu:Nmul_A2633.
    PATRICi22729016. VBINitMul110821_3056.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000103 Genomic DNA. Translation: ABB75920.1 .
    RefSeqi YP_413312.1. NC_007614.1.

    3D structure databases

    ProteinModelPortali Q2Y5Q1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 323848.Nmul_A2633.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB75920 ; ABB75920 ; Nmul_A2633 .
    GeneIDi 3786336.
    KEGGi nmu:Nmul_A2633.
    PATRICi 22729016. VBINitMul110821_3056.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci NMUL323848:GKEC-2679-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. "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC 25196."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25196 / NCIMB 11849.

    Entry informationi

    Entry nameiGLND_NITMU
    AccessioniPrimary (citable) accession number: Q2Y5Q1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 61 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