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 with an iron-sulfur center. In addition to the Rieske center, TphA1 has a binding site for NADPH + H⁺. The catalytic domain oxidizes NADPH + H⁺ and reduces TphA1. Afterwards 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.