Identification
Name:P-protein
Synonyms:
  • Chorismate mutase
  • CM
  • Prephenate dehydratase
  • PDT
Gene Name:pheA
Enzyme Class:
Biological Properties
General Function:Involved in chorismate mutase activity
Specific Function:Chorismate = prephenate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB04030Carbon dioxideMetaboCard
ECMDB12199ChorismateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00159L-PhenylalanineMetaboCard
ECMDB00205Phenylpyruvic acidMetaboCard
ECMDB12283PrephenateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
carbon-oxygen lyase activity
catalytic activity
chorismate mutase activity
hydro-lyase activity
intramolecular transferase activity
isomerase activity
lyase activity
prephenate dehydratase activity
Process
aromatic amino acid family metabolic process
carboxylic acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
chorismate metabolic process
dicarboxylic acid metabolic process
L-phenylalanine biosynthetic process
L-phenylalanine metabolic process
metabolic process
organic acid metabolic process
oxoacid metabolic process
Gene Properties
Blattner:b2599
Gene OrientationClockwise
Centisome Percentage:58.96
Left Sequence End2735767
Right Sequence End2736927
Gene Sequence:
>1161 bp
ATGACAAATAACCCTCTGATTCCACAAAGCAAACTTCCACAACTTGGCACCACTATTTTC
ACCCAGATGAGCGCGCTGGCGCAGCAACACCAGGCGATTAACCTGTCGCAAGGCTTTCCT
GATTTTGATGGTCCGCGCTATTTACAGGAGCGGCTGGCGCACCACGTTGCACAGGGGGCA
AACCAATACGCGCCCATGACCGGCGTGCAGGCCTTGCGCGAGGCGATTGCTCAGAAAACG
GAACGTTTGTATGGCTATCAACCAGATGCCGATAGCGATATCACCGTAACGGCAGGGGCG
ACGGAAGCGTTATACGCGGCGATTACCGCACTGGTGCGCAATGGCGATGAAGTGATTTGT
TTTGATCCCAGCTATGACAGTTACGCCCCCGCCATCGCGCTTTCTGGGGGAATAGTGAAG
CGTATGGCACTGCAACCACCGCATTTTCGCGTTGACTGGCAGGAATTTGCCGCATTATTA
AGCGAGCGCACCAGACTGGTGATCCTCAACACTCCGCATAACCCCAGTGCAACTGTCTGG
CAGCAGGCTGATTTCGCCGCTTTGTGGCAGGCGATCGCCGGGCACGAGATTTTTGTCATT
AGCGATGAAGTCTACGAGCACATCAACTTTTCACAACAGGGCCATGCCAGTGTGCTGGCG
CATCCGCAGCTGCGTGAGCGGGCAGTGGCGGTTTCTTCATTTGGCAAGACCTATCATATG
ACCGGCTGGAAAGTGGGTTATTGTGTTGCGCCAGCGCCCATCAGCGCCGAAATTCGCAAG
GTACATCAGTATCTGACCTTTTCGGTGAATACCCCGGCACAGCTGGCGCTTGCTGATATG
CTACGTGCAGAACCTGAGCATTATCTTGCGTTACCGGACTTTTATCGCCAGAAGCGCGAT
ATTCTGGTGAATGCTTTAAATGAAAGCCGGCTGGAGATTTTACCGTGTGAAGGTACATAC
TTTTTGCTGGTGGATTACAGCGCGGTTTCTACCCTGGATGATGTTGAGTTTTGCCAGTGG
CTGACGCAGGAGCACGGCGTAGCGGCGATTCCGCTGTCGGTGTTTTGCGCCGATCCCTTC
CCACATAAACTGATTCGTCTCTGTTTTGCCAAGAAGGAATCGACGTTGCTGGCAGCAGCT
GAACGCCTGCGCCAGCTTTAG
Protein Properties
Pfam Domain Function:
Protein Residues:386
Protein Molecular Weight:43111
Protein Theoretical pI:7
PDB File:1ECM
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>P-protein
MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLI
TLGKAHHLDAHYITRLFQLIIEDSVLTQQALLQQHLNKINPHSARIAFLGPKGSYSHLAA
RQYAARHFEQFIESGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSI
VGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEK
VAQAKSPHVAALGSEAGGTLYGLQVLERIEANQRQNFTRFVVLARKAINVSDQVPAKTTL
LMATGQQAGALVEALLVLRNHNLIMTRLESRPIHGNPWEEMFYLDIQANLESAEMQKALK
ELGEITRSMKVLGCYPSENVVPVDPT
References
External Links:
ResourceLink
Uniprot ID:P0A9J8
Uniprot Name:PHEA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062217
PDB ID:1ECM
Ecogene ID:EG10707
Ecocyc:EG10707
ColiBase:b2599
Kegg Gene:b2599
EchoBASE ID:EB0701
CCDB:PHEA_ECOLI
BacMap:16130520
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
  • Gavini, N., Davidson, B. E. (1990). "pheAo mutants of Escherichia coli have a defective pheA attenuator." J Biol Chem 265:21532-21535. Pubmed: 2254312
  • 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
  • Hudson, G. S., Davidson, B. E. (1984). "Nucleotide sequence and transcription of the phenylalanine and tyrosine operons of Escherichia coli K12." J Mol Biol 180:1023-1051. Pubmed: 6396419
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837
  • Zhang, S., Pohnert, G., Kongsaeree, P., Wilson, D. B., Clardy, J., Ganem, B. (1998). "Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins." J Biol Chem 273:6248-6253. Pubmed: 9497350
  • Zurawski, G., Brown, K., Killingly, D., Yanofsky, C. (1978). "Nucleotide sequence of the leader region of the phenylalanine operon of Escherichia coli." Proc Natl Acad Sci U S A 75:4271-4275. Pubmed: 360214