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Q1LTN0

- PANC_BAUCH

UniProt

Q1LTN0 - PANC_BAUCH

Protein

Pantothenate synthetase

Gene

panC

Organism
Baumannia cicadellinicola subsp. Homalodisca coagulata
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (30 May 2006)
      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 sitei37 – 371Proton donorUniRule annotation
    Binding sitei61 – 611Beta-alanineUniRule annotation
    Binding sitei61 – 611PantoateUniRule annotation
    Binding sitei155 – 1551PantoateUniRule annotation
    Binding sitei178 – 1781ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi30 – 378ATPUniRule annotation
    Nucleotide bindingi149 – 1524ATPUniRule annotation
    Nucleotide bindingi186 – 1894ATPUniRule 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

    BioCyciBCIC374463:GI6Q-231-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:BCI_0231
    OrganismiBaumannia cicadellinicola subsp. Homalodisca coagulata
    Taxonomic identifieri374463 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia
    ProteomesiUP000002427: Chromosome

    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 – 285285Pantothenate synthetasePRO_0000305403Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi374463.BCI_0231.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1LTN0.
    SMRiQ1LTN0. Positions 1-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pantothenate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0414.
    HOGENOMiHOG000175517.
    KOiK01918.
    OMAiAYMGSTR.
    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.

    Q1LTN0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLIIDNITIL RQTIKQWRKS IQSIALIPTM GNLHDGHMTI VNQGRSHTNI    50
    VIVSIFVNPM QFDREEDLFL YPRTLQSDYE KLHKIGVDAV FVPSVETMYR 100
    DNINCHTFLD VPNLSSILEG IYRPNHFRGV ATIISKLFNL VQPNVVYFGE 150
    KDFQQLVLIR QMVRDMNYDI EIIAVPTVRA NDGLALSSRN SYLTPEQRKI 200
    APKLYQVMQT LVTNLCSGEK NIDVLLNKAA KQLSKFGFTP EILEIRDAIT 250
    LQPITINSKK VVVLFSAWLG KARLIDNTQV SIPKE 285
    Length:285
    Mass (Da):32,539
    Last modified:May 30, 2006 - v1
    Checksum:iE3D1F484A338E507
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000238 Genomic DNA. Translation: ABF14074.1.
    RefSeqiWP_011520417.1. NC_007984.1.
    YP_588684.1. NC_007984.1.

    Genome annotation databases

    EnsemblBacteriaiABF14074; ABF14074; BCI_0231.
    GeneIDi4056175.
    KEGGibci:BCI_0231.
    PATRICi21073963. VBIBauCic75062_0220.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000238 Genomic DNA. Translation: ABF14074.1 .
    RefSeqi WP_011520417.1. NC_007984.1.
    YP_588684.1. NC_007984.1.

    3D structure databases

    ProteinModelPortali Q1LTN0.
    SMRi Q1LTN0. Positions 1-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 374463.BCI_0231.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABF14074 ; ABF14074 ; BCI_0231 .
    GeneIDi 4056175.
    KEGGi bci:BCI_0231.
    PATRICi 21073963. VBIBauCic75062_0220.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00028 ; UER00005 .
    BioCyci BCIC374463:GI6Q-231-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. "Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
      Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
      PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiPANC_BAUCH
    AccessioniPrimary (citable) accession number: Q1LTN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 51 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, Reference proteome

    Documents

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

    External Data

    Dasty 3