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Q6FAM5

- GLND_ACIAD

UniProt

Q6FAM5 - GLND_ACIAD

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      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

    BioCyciASP62977:GJVV-1960-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:ACIAD2079
    OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
    Taxonomic identifieri62977 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
    ProteomesiUP000000430: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 888888Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192713Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi62977.ACIAD2079.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6FAM5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini491 – 58696HDUniRule annotationAdd
    BLAST
    Domaini700 – 78182ACT 1UniRule annotationAdd
    BLAST
    Domaini809 – 88779ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 338338UridylyltransferaseAdd
    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.
    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.

    Q6FAM5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIITSPLLDY VTSHQDIKAI NQWRADVEQQ LQEFYENGYS IRDIVLARSN    50
    LIDEALTFLW KHAGLDQSDL GLFAVGGYGR REMLPYSDVD IMILSENDIS 100
    PEHEKQISGF ISSLWDVGNF KPGTSVRSIQ NCVEQATNDL TVATTLIESR 150
    LITGNPDLAK WPRRIVSQTW TDKTFFDAKM EEQAKRHAQH NNTESNLEPD 200
    IKNAPGGIRD MNQIGWIAKR HFRVNRIYDL VHLGFITEYE LKVLEEAESF 250
    LWEIRHHLHL LSKRDENRLL FDHQREIAAK FGYTRAEGQP VNFAVEQFMK 300
    RYYRTAQQVS TLNEMLLAYF NESVITPRLP NYERKIEEIN ENFKLVDGKL 350
    AVQHHKVFSE NPSAILELFY LLANHPEIEG IRARTLRLLI MAAKRIDQEF 400
    RDNPAHQALF MAIIRSPYRL YDTLVDMKRY GILGNYIPAF GQIMGLMQYD 450
    LFHIYTVDAH TLLLIRNLNR FKEPEFAQHF PVVSSVFQRL ARRDIVYLAA 500
    IFHDIAKGRG GDHSELGAED AIEFCRAHGF TERECKLVAW LIHNHLLMSL 550
    TAQKKDISDP DVIKEFAEKL GDMEHLDYLY TLTVADINAT NPKLWNTWRA 600
    SLMRQLYTYS RDVIRSGLGR PVDYQMLIED TKFSASETLV NEFSLDAVEK 650
    VWQELGDEYF LKESADEIAW HTRAILQHGD NPAPIVLLRA HRQSAQDAVQ 700
    IFIYTQDKPN LFATTVAVLD RMNLDVQDAR IITATKAFSL DTYVVLDRFG 750
    TLLTDPEREH TVKEALIKAL SQSDKYPGLM QRRIPRQLRH FDIENTVDIT 800
    LNPVLQQNMV EISTLDQPGL LARVGGLFMM QGLDIHSAKI ATLGERAEDI 850
    FFVTKKDGQP MTTDEAHIFS AQLKLALDEA SNQIVSQH 888
    Length:888
    Mass (Da):102,208
    Last modified:July 19, 2004 - v1
    Checksum:i1F244D77538E36FC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR543861 Genomic DNA. Translation: CAG68888.1.
    RefSeqiYP_046710.1. NC_005966.1.

    Genome annotation databases

    EnsemblBacteriaiCAG68888; CAG68888; ACIAD2079.
    GeneIDi2881141.
    KEGGiaci:ACIAD2079.
    PATRICi20741848. VBIAciSp98416_1868.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR543861 Genomic DNA. Translation: CAG68888.1 .
    RefSeqi YP_046710.1. NC_005966.1.

    3D structure databases

    ProteinModelPortali Q6FAM5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 62977.ACIAD2079.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG68888 ; CAG68888 ; ACIAD2079 .
    GeneIDi 2881141.
    KEGGi aci:ACIAD2079.
    PATRICi 20741848. VBIAciSp98416_1868.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci ASP62977:GJVV-1960-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. "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
      Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
      Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33305 / BD413 / ADP1.

    Entry informationi

    Entry nameiGLND_ACIAD
    AccessioniPrimary (citable) accession number: Q6FAM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 72 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