DB code: T00025

CATH domain 3.50.50.60 : FAD/NAD(P)-binding domain Catalytic domain
3.40.30.20 : Glutaredoxin
3.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2 Catalytic domain
E.C. 1.14.13.7
CSA 1foh
M-CSA 1foh
MACiE

CATH domain Related DB codes (homologues)
3.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2 D00037 D00041 D00064 D00494
3.50.50.60 : FAD/NAD(P)-binding domain M00163 D00015 D00041 D00042 D00045 D00064 D00071 T00004 T00015 T00017 T00211 T00213 T00233 T00242

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P15245 Phenol 2-monooxygenase
EC 1.14.13.7
Phenol hydroxylase
PF01494 (FAD_binding_3)
PF07976 (Phe_hydrox_dim)
[Graphical View]

KEGG enzyme name
phenol 2-monooxygenase
phenol hydroxylase
phenol o-hydroxylase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P15245 PH2M_TRICU Phenol + NADPH + O(2) = catechol + NADP(+) + H(2)O. Homodimer. Cytoplasm. FAD.

KEGG Pathways
Map code Pathways E.C.
MAP00361 gamma-Hexachlorocyclohexane degradation
MAP00622 Toluene and xylene degradation
MAP00626 Naphthalene and anthracene degradation

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C00146 C00005 C00007 C00080 C00090 C00006 C00001
E.C.
Compound FAD Phenol NADPH O2 H+ Catechol NADP+ H2O
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide aromatic ring (only carbon atom) amide group,amine group,nucleotide others others aromatic ring (only carbon atom) amide group,amine group,nucleotide H2O
ChEBI 16238
15882
16474
15379
26689
27140
15378
18135
18009
15377
PubChem 643975
20488062
996
5884
977
1038
289
5886
22247451
962
1fohA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Bound:IPH Unbound Unbound Unbound Unbound
1fohB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Bound:IPH Unbound Unbound Unbound Unbound
1fohC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Bound:IPH Unbound Unbound Unbound Unbound
1fohD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Bound:IPH Unbound Unbound Unbound Unbound
1fohA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fohB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fohC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fohD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fohA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fohB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fohC03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fohD03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1fohA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 54
1fohB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 54
1fohC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 54
1fohD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 54
1fohA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1fohB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1fohC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1fohD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1fohA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 289
1fohB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 289
1fohC03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 289
1fohD03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 289

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Fig.6
[6]
Fig.8, p.613-614
[8]
Scheme 1, Scheme 2
[11]
Fig.10, Scheme 1

References
[1]
Resource
Comments
Medline ID
PubMed ID 4146224
Journal Eur J Biochem
Year 1973
Volume 35
Pages 386-400
Authors Neujahr HY, Gaal A
Title Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2380181
Journal J Biol Chem
Year 1990
Volume 265
Pages 13687-94
Authors Taylor MG, Massey V
Title Decay of the 4a-hydroxy-FAD intermediate of phenol hydroxylase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8269923
Journal Eur J Biochem
Year 1993
Volume 218
Pages 345-53
Authors Peelen S, Rietjens IM, van Berkel WJ, van Workum WA, Vervoort J
Title 19F-NMR study on the pH-dependent regioselectivity and rate of the ortho-hydroxylation of 3-fluorophenol by phenol hydroxylase from Trichosporon cutaneum. Implications for the reaction mechanism.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8145253
Journal J Mol Biol
Year 1994
Volume 238
Pages 128-30
Authors Enroth C, Huang W, Waters S, Neujahr H, Lindqvist Y, Schneider G
Title Crystallization and preliminary X-ray analysis of phenol hydroxylase from Trichosporon cutaneum.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7851397
Journal Eur J Biochem
Year 1995
Volume 227
Pages 284-91
Authors Peelen S, Rietjens IM, Boersma MG, Vervoort J
Title Conversion of phenol derivatives to hydroxylated products by phenol hydroxylase from Trichosporon cutaneum. A comparison of regioselectivity and rate of conversion with calculated molecular orbital substrate characteristics.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID 98298437
PubMed ID 9634698
Journal Structure
Year 1998
Volume 6
Pages 605-17
Authors Enroth C, Neujahr H, Schneider G, Lindqvist Y
Title 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.
Related PDB 1foh
Related UniProtKB P15245
[7]
Resource
Comments
Medline ID
PubMed ID 11082194
Journal Eur J Biochem
Year 2000
Volume 267
Pages 6832-40
Authors Eppink MH, Cammaart E, Van Wassenaar D, Middelhoven WJ, van Berkel WJ
Title Purification and properties of hydroquinone hydroxylase, a FAD-dependent monooxygenase involved in the catabolism of 4-hydroxybenzoate in Candida parapsilosis CBS604.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12427024
Journal Biochemistry
Year 2002
Volume 41
Pages 13627-36
Authors Xu D, Enroth C, Lindqvist Y, Ballou DP, Massey V
Title Studies of the mechanism of phenol hydroxylase: effect of mutation of proline 364 to serine.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 12653998
Journal Eur J Biochem
Year 2003
Volume 270
Pages 1434-40
Authors Griva E, Pessione E, Divari S, Valetti F, Cavaletto M, Rossi GL, Giunta C
Title Phenol hydroxylase from Acinetobacter radioresistens S13. Isolation and characterization of the regulatory component.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 12752444
Journal Eur J Biochem
Year 2003
Volume 270
Pages 2244-53
Authors Divari S, Valetti F, Caposio P, Pessione E, Cavaletto M, Griva E, Gribaudo G, Gilardi G, Giunta C
Title The oxygenase component of phenol hydroxylase from Acinetobacter radioresistens S13.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 12968028
Journal J Biol Chem
Year 2003
Volume 278
Pages 47545-53
Authors Kirchner U, Westphal AH, M?ller R, van Berkel WJ
Title Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 12925790
Journal Acta Crystallogr D Biol Crystallogr
Year 2003
Volume 59
Pages 1597-602
Authors Enroth C
Title High-resolution structure of phenol hydroxylase and correction of sequence errors.
Related PDB 1pn0
Related UniProtKB

Comments
According to the literature [6] and [8], this enzyme catalyzes the following reactions:
(A) Hydride transfer from NADH to FAD, producing NAD+ and FADH2:
(B) Oxygenation of phenol at FADH2 by O2, giving catechol, FAD and water (H2O):

Created Updated
2004-03-25 2009-02-26