P-protein
Details
- Name
- P-protein
- Synonyms
- 5.4.99.5
- CM
- Gene Name
- pheA
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0019560|P-protein MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLI TLGKAHHLDAHYITRLFQLIIEDSVLTQQALLQQHLNKINPHSARIAFLGPKGSYSHLAA RQYAARHFEQFIESGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSI VGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEK VAQAKSPHVAALGSEAGGTLYGLQVLERIEANQRQNFTRFVVLARKAINVSDQVPAKTTL LMATGQQAGALVEALLVLRNHNLIMTRLESRPIHGNPWEEMFYLDIQANLESAEMQKALK ELGEITRSMKVLGCYPSENVVPVDPT
- Number of residues
- 386
- Molecular Weight
- 43110.945
- Theoretical pI
- 6.68
- GO Classification
- Functionsamino acid binding / chorismate mutase activity / prephenate dehydratase activityProcesseschorismate metabolic process / L-phenylalanine biosynthetic process / tyrosine biosynthetic processComponentscytoplasm
- General Function
- Prephenate dehydratase activity
- Specific Function
- Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0019561|P-protein (pheA) ATGACATCGGAAAACCCGTTACTGGCGCTGCGAGAGAAAATCAGCGCGCTGGATGAAAAA TTATTAGCGTTACTGGCAGAACGGCGCGAACTGGCCGTCGAGGTGGGAAAAGCCAAACTG CTCTCGCATCGCCCGGTACGTGATATTGATCGTGAACGCGATTTGCTGGAAAGATTAATT ACGCTCGGTAAAGCGCACCATCTGGACGCCCATTACATTACTCGCCTGTTCCAGCTCATC ATTGAAGATTCCGTATTAACTCAGCAGGCTTTGCTCCAACAACATCTCAATAAAATTAAT CCGCACTCAGCACGCATCGCTTTTCTCGGCCCCAAAGGTTCTTATTCCCATCTTGCGGCG CGCCAGTATGCTGCCCGTCACTTTGAGCAATTCATTGAAAGTGGCTGCGCCAAATTTGCC GATATTTTTAATCAGGTGGAAACCGGCCAGGCCGACTATGCCGTCGTACCGATTGAAAAT ACCAGCTCCGGTGCCATAAACGACGTTTACGATCTGCTGCAACATACCAGCTTGTCGATT GTTGGCGAGATGACGTTAACTATCGACCATTGTTTGTTGGTCTCCGGCACTACTGATTTA TCCACCATCAATACGGTCTACAGCCATCCGCAGCCATTCCAGCAATGCAGCAAATTCCTT AATCGTTATCCGCACTGGAAGATTGAATATACCGAAAGTACGTCTGCGGCAATGGAAAAG GTTGCACAGGCAAAATCACCGCATGTTGCTGCGTTGGGAAGCGAAGCTGGCGGCACTTTG TACGGTTTGCAGGTACTGGAGCGTATTGAAGCAAATCAGCGACAAAACTTCACCCGATTT GTGGTGTTGGCGCGTAAAGCCATTAACGTGTCTGATCAGGTTCCGGCGAAAACCACGTTG TTAATGGCGACCGGGCAACAAGCCGGTGCGCTGGTTGAAGCGTTGCTGGTACTGCGCAAC CACAATCTGATTATGACCCGTCTGGAATCACGCCCGATTCACGGTAATCCATGGGAAGAG ATGTTCTATCTGGATATTCAGGCCAATCTTGAATCAGCGGAAATGCAAAAAGCATTGAAA GAGTTAGGGGAAATCACCCGTTCAATGAAGGTATTGGGCTGTTACCCAAGTGAGAACGTA GTGCCTGTTGATCCAACCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A9J8 UniProtKB Entry Name PHEA_ECOLI GenBank Protein ID 147173 GenBank Gene ID M10431 - General References
- Hudson GS, Davidson BE: Nucleotide sequence and transcription of the phenylalanine and tyrosine operons of Escherichia coli K12. J Mol Biol. 1984 Dec 25;180(4):1023-51. [Article]
- 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 al.: 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. 1997 Apr 28;4(2):91-113. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Gavini N, Davidson BE: pheAo mutants of Escherichia coli have a defective pheA attenuator. J Biol Chem. 1990 Dec 15;265(35):21532-5. [Article]
- Zurawski G, Brown K, Killingly D, Yanofsky C: Nucleotide sequence of the leader region of the phenylalanine operon of Escherichia coli. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4271-5. [Article]
- Dopheide TA, Crewther P, Davidson BE: Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties. J Biol Chem. 1972 Jul 25;247(14):4447-52. [Article]
- Zhang S, Pohnert G, Kongsaeree P, Wilson DB, Clardy J, Ganem B: Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins. J Biol Chem. 1998 Mar 13;273(11):6248-53. [Article]