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A3M4Q8

- GLND_ACIBT

UniProt

A3M4Q8 - GLND_ACIBT

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
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 2 (02 Sep 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

    BioCyciABAU400667:GI0Q-1462-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:A1S_1474
    OrganismiAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
    Taxonomic identifieri400667 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex
    ProteomesiUP000006737: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 887887Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000114748Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi400667.A1S_1474.

    Structurei

    3D structure databases

    ProteinModelPortaliA3M4Q8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini492 – 58695HDUniRule annotationAdd
    BLAST
    Domaini700 – 78283ACT 1UniRule annotationAdd
    BLAST
    Domaini809 – 88779ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 337337UridylyltransferaseAdd
    BLAST
    Regioni339 – 699361Uridylyl-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.
    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.

    A3M4Q8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MINTSPLLNY VSSHHDIKAI NQWRTDVEKQ LQDSYENGQS IREIIKARSD    50
    LVDEALVFLW KHAELDQSKL GLFAVGGYGR REMLPYSDVD IMILSEDEIS 100
    EENEKRISTF ISSLWDVGNF KPGISVRTIQ SCVEQAATDL TVATTLIEAR 150
    LITGNTQLAK WPRRIVSQTW TDKTFYDAKM AEQAKRYHQH NNTESNLEPD 200
    IKNAPGGIRD INQIGWIAKR HFRVNRIYDL VHLGFISEFE LAVLEEAESF 250
    LWEIRHHLHR LAKRDENRLL FDHQREIAAK FGYVRQEGQP VNYGVEQFMK 300
    RYYRTAQQVS TLNEMLLAYF SESVITPRLP NYERKIEVVN DHFKIVDNKL 350
    AVQHHKIFAE HPSAILELFY ILANRPDIEG IRARTLRLLI LAAKRINQSY 400
    RDNPEHQALF MSIIRSPYRL YDTLVAMKRY GVLGNYIPAF GQIMGLMQYD 450
    LFHIYTVDAH TLLLLRNLNR FREPEFAKEF PVVSSVFQRL ARQDIVFIAA 500
    LFHDIAKGRG GDHSELGAED AIEFGRAHGF TERECKLIAW LIQNHLLMSL 550
    TAQKKDISDP DVVKDFAEKL GDMEHLDYLY TLTVADINAT NPKLWNTWRA 600
    SLMRQLYTHA RDVIRTGLGR PVDYQMLIED TKFAASELLV NNFALADVEK 650
    VWQELGDEYF IKESADEIAW HTQAILKHGD NPEPLVLLRA HRKAAQDAVQ 700
    IFIYTRDQPN LFATTVAVLD RMNLDVQDAK IITASTAFSL DTYVVLDRFG 750
    TLLTDPEREE TVKNALVKAL SQPDQYPGLM QRRIPRQLRH FDIENTVDVT 800
    LNEALQQNMV EISTLDHPGL LARVGGLFMM QGLDIHSARI ATLGERAEDI 850
    FFVTKKDGKP LNHEEVKLFS EKLKAALDEA SNQICQH 887
    Length:887
    Mass (Da):102,126
    Last modified:September 2, 2008 - v2
    Checksum:i5D8D5FB823A833F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000521 Genomic DNA. Translation: ABO11902.2.

    Genome annotation databases

    EnsemblBacteriaiABO11902; ABO11902; A1S_1474.
    PATRICi20719190. VBIAciBau103176_1504.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000521 Genomic DNA. Translation: ABO11902.2 .

    3D structure databases

    ProteinModelPortali A3M4Q8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 400667.A1S_1474.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO11902 ; ABO11902 ; A1S_1474 .
    PATRICi 20719190. VBIAciBau103176_1504.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261778.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci ABAU400667:GI0Q-1462-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. "New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
      Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
      Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17978 / NCDC KC 755.

    Entry informationi

    Entry nameiGLND_ACIBT
    AccessioniPrimary (citable) accession number: A3M4Q8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 59 of the entry and version 2 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