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Protein

Pantothenate synthetase

Gene

panC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.1 Publication

Catalytic activityi

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

Enzyme regulationi

Activation requires a combination of a divalent cation, magnesium or manganese, and a monovalent cation, potassium or ammonium. Above the optimum concentration for activation, magnesium and manganese are rather inhibitory. Also activated by 2-mercaptoethanol, dithiothreitol, cysteine and glutathione. Inhibited by divalent cations (mercury, cobalt, zinc, copper, silver), chelating agents (EDTA, EGTA and o-phenanthroline), and analogs of beta-alanine (taurine, gamma-aminobutyrate, gamma-amino-beta-hydroxybutyrate).1 Publication

Kineticsi

  1. KM=63 µM for pantoate1 Publication
  2. KM=100 µM for ATP1 Publication
  3. KM=150 µM for beta-alanine1 Publication
  4. KM=2000 µM for magnesium1 Publication
  5. KM=5500 µM for manganese1 Publication

    pH dependencei

    Optimum pH is 10. Stable from pH 5.0 to 11.0.1 Publication

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius. Stable up to 37 degrees Celsius and loses activity almost completely when incubated at 60 degrees Celsius for 10 minutes.1 Publication

    Pathway:i(R)-pantothenate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Pantothenate synthetase (panC)
    This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei37 – 371Proton donorBy similarity
    Binding sitei61 – 611Beta-alanineBy similarity
    Binding sitei61 – 611PantoateBy similarity
    Binding sitei155 – 1551PantoateBy similarity
    Binding sitei178 – 1781ATP; via amide nitrogen and carbonyl oxygenBy similarity

    Regions

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

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • identical protein binding Source: IntAct
    • pantoate-beta-alanine ligase activity Source: EcoCyc

    GO - Biological processi

    • pantothenate biosynthetic process from valine Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Pantothenate biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
    ECOL316407:JW0129-MONOMER.
    MetaCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
    BRENDAi6.3.2.1. 2026.
    UniPathwayiUPA00028; UER00005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pantothenate synthetase (EC:6.3.2.1)
    Short name:
    PS
    Alternative name(s):
    Pantoate--beta-alanine ligase
    Pantoate-activating enzyme
    Gene namesi
    Name:panC
    Ordered Locus Names:b0133, JW0129
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11746. panC.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 283283Pantothenate synthetasePRO_0000128229Add
    BLAST

    Proteomic databases

    PaxDbiP31663.
    PRIDEiP31663.

    2D gel databases

    SWISS-2DPAGEP31663.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-545354,EBI-545354
    yfcDP655565EBI-545354,EBI-545346

    Protein-protein interaction databases

    DIPiDIP-10437N.
    IntActiP31663. 11 interactions.
    MINTiMINT-1249237.
    STRINGi511145.b0133.

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43Combined sources
    Helixi7 – 1913Combined sources
    Beta strandi24 – 296Combined sources
    Helixi35 – 373Combined sources
    Helixi38 – 469Combined sources
    Beta strandi49 – 557Combined sources
    Helixi59 – 613Combined sources
    Helixi65 – 706Combined sources
    Helixi75 – 8410Combined sources
    Beta strandi89 – 913Combined sources
    Helixi95 – 984Combined sources
    Beta strandi108 – 1103Combined sources
    Helixi114 – 1163Combined sources
    Helixi119 – 1224Combined sources
    Helixi126 – 14116Combined sources
    Beta strandi144 – 1529Combined sources
    Helixi153 – 16614Combined sources
    Beta strandi171 – 1755Combined sources
    Helixi188 – 1925Combined sources
    Helixi195 – 2006Combined sources
    Helixi203 – 21614Combined sources
    Helixi222 – 23615Combined sources
    Beta strandi239 – 2479Combined sources
    Turni248 – 2503Combined sources
    Beta strandi260 – 26910Combined sources
    Beta strandi272 – 28110Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IHOX-ray1.70A/B1-283[»]
    3GUZX-ray1.67A/B1-176[»]
    ProteinModelPortaliP31663.
    SMRiP31663. Positions 1-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31663.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pantothenate synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0414.
    HOGENOMiHOG000175517.
    InParanoidiP31663.
    KOiK01918.
    OMAiQKDAQQF.
    OrthoDBiEOG6Z6FZ4.
    PhylomeDBiP31663.

    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.

    P31663-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLIIETLPLL RQQIRRLRME GKRVALVPTM GNLHDGHMKL VDEAKARADV
    60 70 80 90 100
    VVVSIFVNPM QFDRPEDLAR YPRTLQEDCE KLNKRKVDLV FAPSVKEIYP
    110 120 130 140 150
    NGTETHTYVD VPGLSTMLEG ASRPGHFRGV STIVSKLFNL VQPDIACFGE
    160 170 180 190 200
    KDFQQLALIR KMVADMGFDI EIVGVPIMRA KDGLALSSRN GYLTAEQRKI
    210 220 230 240 250
    APGLYKVLSS IADKLQAGER DLDEIITIAG QELNEKGFRA DDIQIRDADT
    260 270 280
    LLEVSETSKR AVILVAAWLG DARLIDNKMV ELA
    Length:283
    Mass (Da):31,598
    Last modified:July 1, 1993 - v1
    Checksum:i4246647C6FDAFB20
    GO

    Mass spectrometryi

    Molecular mass is 31601.2±3.4 Da from positions 1 - 283. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L17086 Genomic DNA. Translation: AAA24272.1.
    U00096 Genomic DNA. Translation: AAC73244.1.
    AP009048 Genomic DNA. Translation: BAE76042.1.
    PIRiE64736.
    RefSeqiNP_414675.1. NC_000913.3.
    WP_000905383.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73244; AAC73244; b0133.
    BAE76042; BAE76042; BAE76042.
    GeneIDi944958.
    KEGGieco:b0133.
    PATRICi32115371. VBIEscCol129921_0137.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L17086 Genomic DNA. Translation: AAA24272.1.
    U00096 Genomic DNA. Translation: AAC73244.1.
    AP009048 Genomic DNA. Translation: BAE76042.1.
    PIRiE64736.
    RefSeqiNP_414675.1. NC_000913.3.
    WP_000905383.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IHOX-ray1.70A/B1-283[»]
    3GUZX-ray1.67A/B1-176[»]
    ProteinModelPortaliP31663.
    SMRiP31663. Positions 1-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10437N.
    IntActiP31663. 11 interactions.
    MINTiMINT-1249237.
    STRINGi511145.b0133.

    2D gel databases

    SWISS-2DPAGEP31663.

    Proteomic databases

    PaxDbiP31663.
    PRIDEiP31663.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73244; AAC73244; b0133.
    BAE76042; BAE76042; BAE76042.
    GeneIDi944958.
    KEGGieco:b0133.
    PATRICi32115371. VBIEscCol129921_0137.

    Organism-specific databases

    EchoBASEiEB1696.
    EcoGeneiEG11746. panC.

    Phylogenomic databases

    eggNOGiCOG0414.
    HOGENOMiHOG000175517.
    InParanoidiP31663.
    KOiK01918.
    OMAiQKDAQQF.
    OrthoDBiEOG6Z6FZ4.
    PhylomeDBiP31663.

    Enzyme and pathway databases

    UniPathwayiUPA00028; UER00005.
    BioCyciEcoCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
    ECOL316407:JW0129-MONOMER.
    MetaCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
    BRENDAi6.3.2.1. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP31663.
    PROiP31663.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization and sequence of the Escherichia coli panBCD gene cluster."
      Merkel W.K., Nichols B.P.
      FEMS Microbiol. Lett. 143:247-252(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Enzymological properties of pantothenate synthetase from Escherichia coli B."
      Miyatake K., Nakano Y., Kitaoka S.
      J. Nutr. Sci. Vitaminol. 24:243-253(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, ENZYME REGULATION.
      Strain: B.
    5. "The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily."
      von Delft F., Lewendon A., Dhanaraj V., Blundell T.L., Abell C., Smith A.G.
      Structure 9:439-450(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), MASS SPECTROMETRY, SUBUNIT.

    Entry informationi

    Entry nameiPANC_ECOLI
    AccessioniPrimary (citable) accession number: P31663
    Secondary accession number(s): Q2MCG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: July 22, 2015
    This is version 131 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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.