FAD linked oxidases, C-terminal domain | |||||||||
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![]() p-cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit | |||||||||
Identifiers | |||||||||
Symbol | FAD-oxidase_C | ||||||||
Pfam | PF02913 | ||||||||
Pfam clan | CL0277 | ||||||||
InterPro | IPR004113 | ||||||||
SCOP2 | 1ahu / SCOPe / SUPFAM | ||||||||
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In molecular biology FAD-oxidases are a family of FAD-dependent oxidoreductases. They are flavoproteins that contain a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. The region around the histidine that binds the FAD group is conserved in these enzymes. [1]
FAD linked oxidases, C-terminal domain | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() p-cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit | |||||||||
Identifiers | |||||||||
Symbol | FAD-oxidase_C | ||||||||
Pfam | PF02913 | ||||||||
Pfam clan | CL0277 | ||||||||
InterPro | IPR004113 | ||||||||
SCOP2 | 1ahu / SCOPe / SUPFAM | ||||||||
|
In molecular biology FAD-oxidases are a family of FAD-dependent oxidoreductases. They are flavoproteins that contain a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. The region around the histidine that binds the FAD group is conserved in these enzymes. [1]