InterPro : IPR012941

Name  Phenol hydroxylase, C-terminal dimerisation domain Short Name  Phe_hydrox_C_dim_dom
Type  Domain Description  Phenol hydroxylase is a homodimer which hydroxylates phenol to catechol, or similar products. The enzyme is comprised of three domains. The first two domains form the active site. The third domain, this domain, is involved in forming the dimerisation interface. The domain adopts a thioredoxin-like fold []. Protein containing this domain also include 3-hydroxybenzoate 4-monooxygenase from Comamonas testosteroni [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

1 Parent Features

Id Name Short Name Type
IPR012336 Thioredoxin-like fold Thioredoxin-like_fold Domain

2 Publications

First Author Title Year Journal Volume Pages
Enroth C The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis. 1998 Structure 6 605-17
Chang HK Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase. 2008 Biochem Biophys Res Commun 371 149-53

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)