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Q82EC8

- PANC_STRAW

UniProt

Q82EC8 - PANC_STRAW

Protein

Pantothenate synthetase

Gene

panC

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 sitei34 – 341Proton donorUniRule annotation
    Binding sitei61 – 611Beta-alanineUniRule annotation
    Binding sitei61 – 611PantoateUniRule annotation
    Binding sitei154 – 1541PantoateUniRule annotation
    Binding sitei177 – 1771ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi27 – 348ATPUniRule 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

    BioCyciSAVE227882:GJU1-4741-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:SAV_4687
    OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
    Taxonomic identifieri227882 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
    ProteomesiUP000000428: 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 – 333333Pantothenate synthetasePRO_0000305563Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi227882.SAV_4687.

    Structurei

    3D structure databases

    ProteinModelPortaliQ82EC8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pantothenate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0414.
    HOGENOMiHOG000175516.
    KOiK01918.
    OMAiGGEPQVR.
    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]
    PfamiPF02569. Pantoate_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00018. panC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q82EC8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTTLLRTAD ELHARVRHGR RAVVMTMGAL HEGHATLIRT AREIAGAEGE    50
    VVVTVFVNPL QFGRGEDLDR YPRTLDADLK IAEAAGADVV FAPSADEVYP 100
    GGEPQVRISA GPMGERLEGA FRPGHFDGML TVVGKLLHLT RPDVALYGQK 150
    DAQQLALIRR MARDLNFGVE IVGVPTVRED DGLALSSRNR YLAADERRTA 200
    LALSQALFAG RDRHAAQEAL RARAREVPAT RARAEALSAI GESRAAADAH 250
    AVAKATPAGT SGPAAVRCAA RLVLEEAARL QPPLVLDYLG LVDPSDFTEI 300
    PDDFTGEAVL AVAARVGTTR LIDNIPLTFG AAS 333
    Length:333
    Mass (Da):35,472
    Last modified:June 1, 2003 - v1
    Checksum:i6CC22E59257E85D8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000030 Genomic DNA. Translation: BAC72399.1.
    RefSeqiNP_825864.1. NC_003155.4.

    Genome annotation databases

    EnsemblBacteriaiBAC72399; BAC72399; SAV_4687.
    GeneIDi1211045.
    KEGGisma:SAV_4687.
    PATRICi23723249. VBIStrAve112782_5003.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000030 Genomic DNA. Translation: BAC72399.1 .
    RefSeqi NP_825864.1. NC_003155.4.

    3D structure databases

    ProteinModelPortali Q82EC8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 227882.SAV_4687.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC72399 ; BAC72399 ; SAV_4687 .
    GeneIDi 1211045.
    KEGGi sma:SAV_4687.
    PATRICi 23723249. VBIStrAve112782_5003.

    Phylogenomic databases

    eggNOGi COG0414.
    HOGENOMi HOG000175516.
    KOi K01918.
    OMAi GGEPQVR.
    OrthoDBi EOG6Z6FZ4.

    Enzyme and pathway databases

    UniPathwayi UPA00028 ; UER00005 .
    BioCyci SAVE227882:GJU1-4741-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 ]
    Pfami PF02569. Pantoate_ligase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00018. panC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
      Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
      Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
    2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
      Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
      Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

    Entry informationi

    Entry nameiPANC_STRAW
    AccessioniPrimary (citable) accession number: Q82EC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 68 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