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Q5WTD6

- PANC_LEGPL

UniProt

Q5WTD6 - PANC_LEGPL

Protein

Pantothenate synthetase

Gene

panC

Organism
Legionella pneumophila (strain Lens)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.UniRule annotation

    Catalytic activityi

    ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei36 – 361Proton donorUniRule annotation
    Binding sitei60 – 601Beta-alanineUniRule annotation
    Binding sitei60 – 601PantoateUniRule annotation
    Binding sitei152 – 1521PantoateUniRule annotation
    Binding sitei175 – 1751ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi29 – 368ATPUniRule annotation
    Nucleotide bindingi146 – 1494ATPUniRule annotation
    Nucleotide bindingi183 – 1864ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. pantoate-beta-alanine ligase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. pantothenate biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Pantothenate biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciLPNE297245:GJD4-2802-MONOMER.
    UniPathwayiUPA00028; UER00005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pantothenate synthetaseUniRule annotation (EC:6.3.2.1UniRule annotation)
    Short name:
    PSUniRule annotation
    Alternative name(s):
    Pantoate--beta-alanine ligaseUniRule annotation
    Pantoate-activating enzymeUniRule annotation
    Gene namesi
    Name:panCUniRule annotation
    Ordered Locus Names:lpl2589
    OrganismiLegionella pneumophila (strain Lens)
    Taxonomic identifieri297245 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
    ProteomesiUP000002517: Chromosome

    Organism-specific databases

    LegioListilpl2589.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 252252Pantothenate synthetasePRO_0000305468Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi297245.lpl2589.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5WTD6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pantothenate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0414.
    HOGENOMiHOG000175517.
    KOiK01918.
    OMAiASSKENH.
    OrthoDBiEOG6Z6FZ4.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00158. PanC.
    InterProiIPR003721. Pantoate_ligase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
    PfamiPF02569. Pantoate_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00018. panC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q5WTD6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQIFHNLNEW IRFRNSLSPD LSLGFAPTMG NLHAGHASLF LASSKENHYT    50
    VSSLFVNPTQ FNNPDDYKHY PRTVDADLEL MTQNGVDFCI LPNENEIYAD 100
    GYAYQVQENR FGQLMEGKHR PGHFNGVLTI VMKLFNLVKP TRAYFGEKDY 150
    QQLLLIQGMV KALFMDIEIK SCPTVREKSG LACSSRNNRL TPSQREIADE 200
    FAKIFHQNKS SAMISKELEA LGITVEYIEE FQGRRFAAVK IGDIRLIDNY 250
    LL 252
    Length:252
    Mass (Da):28,822
    Last modified:November 23, 2004 - v1
    Checksum:i259F2DC8BAA7D232
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628337 Genomic DNA. Translation: CAH16830.1.
    RefSeqiWP_011216532.1. NC_006369.1.
    YP_127917.1. NC_006369.1.

    Genome annotation databases

    EnsemblBacteriaiCAH16830; CAH16830; lpl2589.
    GeneIDi3115574.
    KEGGilpf:lpl2589.
    PATRICi22319068. VBILegPne33733_2842.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628337 Genomic DNA. Translation: CAH16830.1 .
    RefSeqi WP_011216532.1. NC_006369.1.
    YP_127917.1. NC_006369.1.

    3D structure databases

    ProteinModelPortali Q5WTD6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 297245.lpl2589.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH16830 ; CAH16830 ; lpl2589 .
    GeneIDi 3115574.
    KEGGi lpf:lpl2589.
    PATRICi 22319068. VBILegPne33733_2842.

    Organism-specific databases

    LegioListi lpl2589.

    Phylogenomic databases

    eggNOGi COG0414.
    HOGENOMi HOG000175517.
    KOi K01918.
    OMAi ASSKENH.
    OrthoDBi EOG6Z6FZ4.

    Enzyme and pathway databases

    UniPathwayi UPA00028 ; UER00005 .
    BioCyci LPNE297245:GJD4-2802-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    HAMAPi MF_00158. PanC.
    InterProi IPR003721. Pantoate_ligase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR21299:SF1. PTHR21299:SF1. 1 hit.
    Pfami PF02569. Pantoate_ligase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00018. panC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
      Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
      Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Lens.

    Entry informationi

    Entry nameiPANC_LEGPL
    AccessioniPrimary (citable) accession number: Q5WTD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The reaction proceeds by a bi uni uni bi ping pong mechanism.UniRule annotation

    Keywords - Technical termi

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3