Part:BBa_K808011

tphA1: reduces the tphA2A3 complex

Figure 1. Homology modelling of TphA1. For simulation parameters http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA1 click here.

TphA1 is coding for the terephthalate dioxygenase reductase from Comamonas testosteroni KF-1. TphA1 forms together with tphA2 and tphA3 the terephthalic acid 1,2-dioxigenase system (TERDOS). TERDOS catalyzes the first reaction in the terephthalic acid degradation.

Usage and Biology

TphA1 is just like TphA2 an rieske protein. In addition to the rieske center, TphA1 has a binding site for NADPH + H⁺. The catalytic domäne oxidizes NADPH + H⁺ and reduces TphA1. Now the reduced TphA1 reduces the TphA2A3 complex.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  INCOMPATIBLE WITH RFC[12]

  Illegal NheI site found at 954
  
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 85
  Illegal NgoMIV site found at 394
  
• 1000
  COMPATIBLE WITH RFC[1000]

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.