Literature summary for 1.14.15.25 extracted from

Dutta, T.; Chakraborty, J.; Roy, M.; Ghosal, D.; Khara, P.; Gunsalus, I.
Cloning and characterization of a p-cymene monooxygenase from Pseudomonas chlororaphis subsp. aureofaciens (2010), Res. Microbiol., 161, 876-882 .

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Organism

Organism	UniProt	Comment	Textmining
Pseudomonas chlororaphis subsp. aureofaciens	P95461 and O84920 and O84919	P95461 i.e. subunit CymA, O84920 i.e. subunit CymB, O84919 i.e. subunit CymM	-

Synonyms

Synonyms	Comment	Organism
cymA	-	Pseudomonas chlororaphis subsp. aureofaciens
CymB	-	Pseudomonas chlororaphis subsp. aureofaciens
CymM	-	Pseudomonas chlororaphis subsp. aureofaciens

General Information

General Information	Comment	Organism
physiological function	expression of all three components (cymMBA) in Escherichia coli leads to p-cymene methyl group hydroxylation, while expression of cymM and cymA along with the partially truncated cymB gene shows an 85% decrease in the hydroxylation capacity. The CymM gene product shows similarity to integral-membrane di-iron enzymes, while that CymB shows no significant similarity to other known proteins	Pseudomonas chlororaphis subsp. aureofaciens

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Release 2023.1 (January 2023)