Identification
Name:Pantothenate synthetase
Synonyms:
  • PS
  • Pantoate--beta-alanine ligase
  • Pantoate-activating enzyme
Gene Name:panC
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate
Cellular Location:Cytoplasm (Potential)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
Thumb+Thumb+(R)-pantoate+ThumbThumb+Pyrophosphate+Thumb+Pantothenic acid+Thumb
Thumb+ThumbThumb+Pyrophosphate+Thumb
EcoCyc Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB20016(R)-PantoateMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00056beta-AlanineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00210Pantothenic acidMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Function
acid-amino acid ligase activity
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
pantoate-beta-alanine ligase activity
Process
biosynthetic process
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
pantothenate biosynthetic process
Gene Properties
Blattner:b0133
Gene OrientationCounterclockwise
Centisome Percentage:3.19
Left Sequence End147944
Right Sequence End148795
Gene Sequence:
>852 bp
GTGTTAATTATCGAAACCCTGCCGCTGCTGCGTCAGCAAATTCGCCGCCTGCGTATGGAA
GGCAAGCGCGTGGCGCTGGTGCCTACCATGGGTAACCTGCACGATGGCCATATGAAGCTG
GTCGACGAAGCCAAAGCCCGCGCCGATGTGGTCGTCGTCAGTATTTTCGTTAACCCGATG
CAGTTCGACCGCCCGGAAGATCTGGCTCGTTATCCACGGACCTTGCAGGAGGACTGCGAG
AAGCTAAACAAACGTAAAGTGGATTTAGTTTTCGCCCCTTCGGTAAAAGAGATCTACCCG
AACGGTACTGAAACCCACACTTACGTTGACGTTCCTGGCCTTTCGACCATGCTGGAAGGT
GCCAGCCGTCCGGGACATTTTCGCGGCGTTTCGACTATTGTCAGCAAGCTGTTCAACCTG
GTCCAGCCGGACATCGCCTGCTTCGGTGAAAAAGATTTTCAGCAACTGGCGCTGATCCGC
AAAATGGTTGCCGATATGGGCTTCGATATTGAGATTGTCGGTGTGCCAATTATGCGCGCC
AAAGACGGTCTGGCGCTAAGTTCCCGTAACGGTTATCTGACGGCGGAACAACGCAAAATT
GCGCCTGGTCTGTACAAAGTTTTAAGTTCGATTGCTGACAAATTGCAGGCTGGGGAACGG
GATCTCGATGAAATTATTACCATTGCGGGGCAAGAACTGAATGAAAAAGGCTTCCGCGCC
GATGATATTCAGATTCGCGATGCCGACACATTGCTGGAAGTTTCTGAAACCAGCAAACGG
GCAGTAATTCTGGTAGCCGCCTGGCTTGGCGATGCTCGCCTGATCGACAACAAAATGGTC
GAGCTGGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:283
Protein Molecular Weight:31597
Protein Theoretical pI:6
PDB File:1IHO
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Pantothenate synthetase
MLIIETLPLLRQQIRRLRMEGKRVALVPTMGNLHDGHMKLVDEAKARADVVVVSIFVNPM
QFDRPEDLARYPRTLQEDCEKLNKRKVDLVFAPSVKEIYPNGTETHTYVDVPGLSTMLEG
ASRPGHFRGVSTIVSKLFNLVQPDIACFGEKDFQQLALIRKMVADMGFDIEIVGVPIMRA
KDGLALSSRNGYLTAEQRKIAPGLYKVLSSIADKLQAGERDLDEIITIAGQELNEKGFRA
DDIQIRDADTLLEVSETSKRAVILVAAWLGDARLIDNKMVELA
References
External Links:
ResourceLink
Uniprot ID:P31663
Uniprot Name:PANC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674348
PDB ID:1IHO
Ecogene ID:EG11746
Ecocyc:EG11746
ColiBase:b0133
Kegg Gene:b0133
EchoBASE ID:EB1696
CCDB:PANC_ECOLI
BacMap:16128126
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Merkel, W. K., Nichols, B. P. (1996). "Characterization and sequence of the Escherichia coli panBCD gene cluster." FEMS Microbiol Lett 143:247-252. Pubmed: 8837478
  • Miyatake, K., Nakano, Y., Kitaoka, S. (1978). "Enzymological properties of pantothenate synthetase from Escherichia coli B." J Nutr Sci Vitaminol (Tokyo) 24:243-253. Pubmed: 357689
  • von Delft, F., Lewendon, A., Dhanaraj, V., Blundell, T. L., Abell, C., Smith, A. G. (2001). "The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily." Structure 9:439-450. Pubmed: 11377204