Part:BBa_K808012

tphA2: Catalyzes together with tphA3 TPA to DCD

Figure 1. Homology modelling of TphA2. For simulation parameters http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA3 click here.

TphA2 is coding for the lagre terephthalate 1,2-dioxygenase subunit from Comamonas testosteroni KF-1. TphA2 forms together with TphA1 and TphA3 the terephthalic acid 1,2-dioxygenase system (TERDOS). TERDOS catalyzes the first reaction in the terephthalic acid degradation.

Usage and Biology

TphA2 consists of 414 amino acids and has a molar mass of 46.35 kDa. It is a Rieske protein with a iron-sulfuric center. The Rieske center is located in the active site and is typical for oxygenases. Figure 1 shows TphA1 with the Rieske center.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 390
  
• 1000
  INCOMPATIBLE WITH RFC[1000]

  Illegal SapI.rc site found at 409
  

References

• Sasoh, M., E. Masai, et al. (2006). "Characterization of the terephthalate degradation genes of Comamonas sp. strain E6." Appl Environ Microbiol 72(3): 1825-1832.
• Fukuhara, Y., K. Inakazu, et al. (2010). "Characterization of the isophthalate degradation genes of Comamonas sp. strain E6." Appl Environ Microbiol 76(2): 519-527.
• Kamimura, N., T. Aoyama, et al. (2010). "Characterization of the protocatechuate 4,5-cleavage pathway operon in Comamonas sp. strain E6 and discovery of a novel pathway gene." Appl Environ Microbiol 76(24): 8093-8101.
• Schläfli HR, Weiss MA, Leisinger T, Cook AM. (1994)"Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2: purification and some properties of the oxygenase component." J Bacteriol. 1994 Nov;176(21):6644-52.