Difference between revisions of "Part:BBa K3823011"
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| + | There is a SQR (Sulfide: quinone oxidoreductase) from <i>C. pinatubonensis</i>. | ||
Sulfide: quinone oxidoreductase, is an ancient flavoprotein of the disulfide oxidoreductase family that is present in nearly all domains of life. SQRs were first found in sulfide trophic bacteria, later SQR-like enzymes were found in the mitochondria of some fungi, as well as in all animal species whose genomes have been sequenced. Several SQRs have been purified and characterized by biochemical methods. They are considered to be integral monotopic membrane proteins, associating with the membrane through amphipathic helices. The monomeric molecular mass of the enzyme is around 50 kDa. The enzyme usually harbors a covalently-bound FAD cofactor in each monomer<sup>[1,2]</sup>. | Sulfide: quinone oxidoreductase, is an ancient flavoprotein of the disulfide oxidoreductase family that is present in nearly all domains of life. SQRs were first found in sulfide trophic bacteria, later SQR-like enzymes were found in the mitochondria of some fungi, as well as in all animal species whose genomes have been sequenced. Several SQRs have been purified and characterized by biochemical methods. They are considered to be integral monotopic membrane proteins, associating with the membrane through amphipathic helices. The monomeric molecular mass of the enzyme is around 50 kDa. The enzyme usually harbors a covalently-bound FAD cofactor in each monomer<sup>[1,2]</sup>. | ||
Revision as of 09:28, 21 October 2021
Sqr from C. pinatubonensis
There is a SQR (Sulfide: quinone oxidoreductase) from C. pinatubonensis.
Sulfide: quinone oxidoreductase, is an ancient flavoprotein of the disulfide oxidoreductase family that is present in nearly all domains of life. SQRs were first found in sulfide trophic bacteria, later SQR-like enzymes were found in the mitochondria of some fungi, as well as in all animal species whose genomes have been sequenced. Several SQRs have been purified and characterized by biochemical methods. They are considered to be integral monotopic membrane proteins, associating with the membrane through amphipathic helices. The monomeric molecular mass of the enzyme is around 50 kDa. The enzyme usually harbors a covalently-bound FAD cofactor in each monomer[1,2].
References
- [1] Wakai, S., et al., Purification and characterization of sulfide : quinone oxidoreductase from an acidophilic iron-oxidizing bacterium, acidithiobacillus ferrooxidans.Bioscience Biotechnology and Biochemistry, 2007. 71(11): p. 2735-2742.
- [2]Zhang, Y. and J.H.Weiner, Characterization of the kinetics and electron paramagnetic resonance spectroscopic properties of Acidithiobacillus ferrooxidans sulfide:quinone oxidoreductase (SQR). Archives of Biochemistry and Biophysics, 2014. 564: p. 110-119.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 175
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 175
Illegal NotI site found at 364
Illegal NotI site found at 413 - 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 540
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 175
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 175
Illegal NgoMIV site found at 370
Illegal NgoMIV site found at 931
Illegal NgoMIV site found at 982
Illegal NgoMIV site found at 1056
Illegal NgoMIV site found at 1270
Illegal NgoMIV site found at 1342 - 1000COMPATIBLE WITH RFC[1000]