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P31663

- PANC_ECOLI

UniProt

P31663 - PANC_ECOLI

Protein

Pantothenate synthetase

Gene

panC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      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.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

    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

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. pantoate-beta-alanine ligase activity Source: EcoCyc
    4. protein binding Source: IntAct

    GO - Biological processi

    1. pantothenate biosynthetic process from valine Source: EcoCyc

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11746. panC.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP31663.

    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 – 43
    Helixi7 – 1913
    Beta strandi24 – 296
    Helixi35 – 373
    Helixi38 – 469
    Beta strandi49 – 557
    Helixi59 – 613
    Helixi65 – 706
    Helixi75 – 8410
    Beta strandi89 – 913
    Helixi95 – 984
    Beta strandi108 – 1103
    Helixi114 – 1163
    Helixi119 – 1224
    Helixi126 – 14116
    Beta strandi144 – 1529
    Helixi153 – 16614
    Beta strandi171 – 1755
    Helixi188 – 1925
    Helixi195 – 2006
    Helixi203 – 21614
    Helixi222 – 23615
    Beta strandi239 – 2479
    Turni248 – 2503
    Beta strandi260 – 26910
    Beta strandi272 – 28110

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP31663.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pantothenate synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0414.
    HOGENOMiHOG000175517.
    KOiK01918.
    OMAiECPIVRE.
    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

    MLIIETLPLL RQQIRRLRME GKRVALVPTM GNLHDGHMKL VDEAKARADV    50
    VVVSIFVNPM QFDRPEDLAR YPRTLQEDCE KLNKRKVDLV FAPSVKEIYP 100
    NGTETHTYVD VPGLSTMLEG ASRPGHFRGV STIVSKLFNL VQPDIACFGE 150
    KDFQQLALIR KMVADMGFDI EIVGVPIMRA KDGLALSSRN GYLTAEQRKI 200
    APGLYKVLSS IADKLQAGER DLDEIITIAG QELNEKGFRA DDIQIRDADT 250
    LLEVSETSKR AVILVAAWLG DARLIDNKMV ELA 283
    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:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488436.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73244; AAC73244; b0133.
    BAE76042; BAE76042; BAE76042.
    GeneIDi12932172.
    944958.
    KEGGiecj:Y75_p0130.
    eco:b0133.
    PATRICi32115371. VBIEscCol129921_0137.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L17086 Genomic DNA. Translation: AAA24272.1 .
    U00096 Genomic DNA. Translation: AAC73244.1 .
    AP009048 Genomic DNA. Translation: BAE76042.1 .
    PIRi E64736.
    RefSeqi NP_414675.1. NC_000913.3.
    YP_488436.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IHO X-ray 1.70 A/B 1-283 [» ]
    3GUZ X-ray 1.67 A/B 1-176 [» ]
    ProteinModelPortali P31663.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10437N.
    IntActi P31663. 11 interactions.
    MINTi MINT-1249237.
    STRINGi 511145.b0133.

    2D gel databases

    SWISS-2DPAGE P31663.

    Proteomic databases

    PaxDbi P31663.
    PRIDEi P31663.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73244 ; AAC73244 ; b0133 .
    BAE76042 ; BAE76042 ; BAE76042 .
    GeneIDi 12932172.
    944958.
    KEGGi ecj:Y75_p0130.
    eco:b0133.
    PATRICi 32115371. VBIEscCol129921_0137.

    Organism-specific databases

    EchoBASEi EB1696.
    EcoGenei EG11746. panC.

    Phylogenomic databases

    eggNOGi COG0414.
    HOGENOMi HOG000175517.
    KOi K01918.
    OMAi ECPIVRE.
    OrthoDBi EOG6Z6FZ4.
    PhylomeDBi P31663.

    Enzyme and pathway databases

    UniPathwayi UPA00028 ; UER00005 .
    BioCyci EcoCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.
    ECOL316407:JW0129-MONOMER.
    MetaCyc:PANTOATE-BETA-ALANINE-LIG-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P31663.
    PROi P31663.

    Gene expression databases

    Genevestigatori P31663.

    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. "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: October 1, 2014
    This is version 124 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