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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

    Pathwayi: (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)DescriptionActionsGraphical viewLength
    Active sitei37Proton donorBy similarity1
    Binding sitei61Beta-alanineBy similarity1
    Binding sitei61PantoateBy similarity1
    Binding sitei155PantoateBy similarity1
    Binding sitei178ATP; via amide nitrogen and carbonyl oxygenBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi30 – 37ATPBy similarity8
    Nucleotide bindingi149 – 152ATPBy similarity4
    Nucleotide bindingi186 – 189ATPBy similarity4

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 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)DescriptionActionsGraphical viewLength
    ChainiPRO_00001282291 – 283Pantothenate synthetaseAdd BLAST283

    Proteomic databases

    EPDiP31663.
    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

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi4261166. 135 interactors.
    DIPiDIP-10437N.
    IntActiP31663. 11 interactors.
    MINTiMINT-1249237.
    STRINGi511145.b0133.

    Structurei

    Secondary structure

    1283
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 4Combined sources3
    Helixi7 – 19Combined sources13
    Beta strandi24 – 29Combined sources6
    Helixi35 – 37Combined sources3
    Helixi38 – 46Combined sources9
    Beta strandi49 – 55Combined sources7
    Helixi59 – 61Combined sources3
    Helixi65 – 70Combined sources6
    Helixi75 – 84Combined sources10
    Beta strandi89 – 91Combined sources3
    Helixi95 – 98Combined sources4
    Beta strandi108 – 110Combined sources3
    Helixi114 – 116Combined sources3
    Helixi119 – 122Combined sources4
    Helixi126 – 141Combined sources16
    Beta strandi144 – 152Combined sources9
    Helixi153 – 166Combined sources14
    Beta strandi171 – 175Combined sources5
    Helixi188 – 192Combined sources5
    Helixi195 – 200Combined sources6
    Helixi203 – 216Combined sources14
    Helixi222 – 236Combined sources15
    Beta strandi239 – 247Combined sources9
    Turni248 – 250Combined sources3
    Beta strandi260 – 269Combined sources10
    Beta strandi272 – 281Combined sources10

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP31663.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pantothenate synthetase family.Curated

    Phylogenomic databases

    eggNOGiENOG4107R03. Bacteria.
    COG0414. LUCA.
    HOGENOMiHOG000175517.
    InParanoidiP31663.
    KOiK01918.
    OMAiENVDCIF.
    PhylomeDBiP31663.

    Family and domain databases

    CDDicd00560. PanC. 1 hit.
    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00158. PanC. 1 hit.
    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_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73244; AAC73244; b0133.
    BAE76042; BAE76042; BAE76042.
    GeneIDi944958.
    KEGGiecj:JW0129.
    eco: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_LN832404.1.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi4261166. 135 interactors.
    DIPiDIP-10437N.
    IntActiP31663. 11 interactors.
    MINTiMINT-1249237.
    STRINGi511145.b0133.

    2D gel databases

    SWISS-2DPAGEP31663.

    Proteomic databases

    EPDiP31663.
    PaxDbiP31663.
    PRIDEiP31663.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73244; AAC73244; b0133.
    BAE76042; BAE76042; BAE76042.
    GeneIDi944958.
    KEGGiecj:JW0129.
    eco:b0133.
    PATRICi32115371. VBIEscCol129921_0137.

    Organism-specific databases

    EchoBASEiEB1696.
    EcoGeneiEG11746. panC.

    Phylogenomic databases

    eggNOGiENOG4107R03. Bacteria.
    COG0414. LUCA.
    HOGENOMiHOG000175517.
    InParanoidiP31663.
    KOiK01918.
    OMAiENVDCIF.
    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

    CDDicd00560. PanC. 1 hit.
    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00158. PanC. 1 hit.
    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...

    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: November 2, 2016
    This is version 137 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

    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 one 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.