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Q4LA34

- PANC_STAHJ

UniProt

Q4LA34 - PANC_STAHJ

Protein

Pantothenate synthetase

Gene

panC

Organism
Staphylococcus haemolyticus (strain JCSC1435)
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 (02 Aug 2005)
      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 sitei38 – 381Proton donorUniRule annotation
    Binding sitei62 – 621Beta-alanineUniRule annotation
    Binding sitei62 – 621PantoateUniRule annotation
    Binding sitei154 – 1541PantoateUniRule annotation
    Binding sitei177 – 1771ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi31 – 388ATPUniRule annotation
    Nucleotide bindingi148 – 1514ATPUniRule annotation
    Nucleotide bindingi185 – 1884ATPUniRule 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

    BioCyciSHAE279808:GJX7-184-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:SH0182
    OrganismiStaphylococcus haemolyticus (strain JCSC1435)
    Taxonomic identifieri279808 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000543: 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 – 283283Pantothenate synthetasePRO_0000128277Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi279808.SH0182.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4LA34.
    SMRiQ4LA34. Positions 3-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pantothenate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0414.
    HOGENOMiHOG000175517.
    KOiK01918.
    OMAiIVRDSDH.
    OrthoDBiEOG6Z6FZ4.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00158. PanC.
    InterProiIPR004821. Cyt_trans-like.
    IPR003721. Pantoate_ligase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
    PfamiPF02569. Pantoate_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
    TIGR00018. panC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q4LA34-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKVIQTVSE MQQITQELKS TGKTIGFVPT MGALHEGHLS MMRRSVEEND    50
    ITVISVFVNP LQFGPNEDFD AYPRQIDQDV ALVEAINVDY VFHPAVEEMY 100
    PNELSVTLKV GRLAEVLEGA QRPGHFDGVV TVLNKLFNIV SPNKAYFGKK 150
    DAQQLAIVEK MVEDFNHPIQ IVGIDIVREE DGLARSSRNV YLTDDERQEA 200
    VHLSKSLEIA QTLYKQGERR SHIIVGEIKT YLSEHTSGHI DEVAIYSYPD 250
    LEVATEIQGQ IFISLAVKFS KARLIDNIIL GSE 283
    Length:283
    Mass (Da):31,756
    Last modified:August 2, 2005 - v1
    Checksum:iB4BAADAB5FD37F47
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006716 Genomic DNA. Translation: BAE03491.1.
    RefSeqiWP_011274511.1. NC_007168.1.
    YP_252097.1. NC_007168.1.

    Genome annotation databases

    EnsemblBacteriaiBAE03491; BAE03491; SH0182.
    GeneIDi3482012.
    KEGGisha:SH0182.
    PATRICi19616399. VBIStaHae67511_0176.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006716 Genomic DNA. Translation: BAE03491.1 .
    RefSeqi WP_011274511.1. NC_007168.1.
    YP_252097.1. NC_007168.1.

    3D structure databases

    ProteinModelPortali Q4LA34.
    SMRi Q4LA34. Positions 3-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 279808.SH0182.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAE03491 ; BAE03491 ; SH0182 .
    GeneIDi 3482012.
    KEGGi sha:SH0182.
    PATRICi 19616399. VBIStaHae67511_0176.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00028 ; UER00005 .
    BioCyci SHAE279808:GJX7-184-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    HAMAPi MF_00158. PanC.
    InterProi IPR004821. Cyt_trans-like.
    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 TIGR00125. cyt_tran_rel. 1 hit.
    TIGR00018. panC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
      Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
      J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JCSC1435.

    Entry informationi

    Entry nameiPANC_STAHJ
    AccessioniPrimary (citable) accession number: Q4LA34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: August 2, 2005
    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