DB code: D00064

CATH domain 3.50.50.60 : FAD/NAD(P)-binding domain
3.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2 Catalytic domain
E.C. 1.14.13.2
CSA 1dod
M-CSA 1dod
MACiE M0131

CATH domain Related DB codes (homologues)
3.50.50.60 : FAD/NAD(P)-binding domain M00163 D00015 D00041 D00042 D00045 D00071 T00004 T00015 T00017 T00025 T00211 T00213 T00233 T00242
3.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2 D00037 D00041 D00494 T00025

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P20586 p-hydroxybenzoate hydroxylase
PHBH
EC 1.14.13.2
4-hydroxybenzoate 3-monooxygenase
NP_248938.1 (Protein)
NC_002516.2 (DNA/RNA sequence)
PF01494 (FAD_binding_3)
[Graphical View]
P00438 p-hydroxybenzoate hydroxylase
EC 1.14.13.2
4-hydroxybenzoate 3-monooxygenase
PF01494 (FAD_binding_3)
[Graphical View]

KEGG enzyme name
4-hydroxybenzoate 3-monooxygenase
p-hydroxybenzoate hydrolyase
p-hydroxybenzoate hydroxylase
4-hydroxybenzoate 3-hydroxylase
4-hydroxybenzoate monooxygenase
4-hydroxybenzoic hydroxylase
p-hydroxybenzoate-3-hydroxylase
p-hydroxybenzoic acid hydrolase
p-hydroxybenzoic acid hydroxylase
p-hydroxybenzoic hydroxylase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00438 PHHY_PSEFL 4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O. Homodimer. FAD.
P20586 PHHY_PSEAE 4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O. Homodimer. FAD.

KEGG Pathways
Map code Pathways E.C.
MAP00623 2,4-Dichlorobenzoate degradation
MAP00362 Benzoate degradation via hydroxylation

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C00156 C00005 C00007 C00080 C00230 C00006 C00001
E.C.
Compound FAD 4-Hydroxybenzoate NADPH O2 H+ Protocatechuate NADP+ H2O Flavin 4a-hydroperoxide intermediate Flavin 4a-hydroxide intermediate
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide aromatic ring (only carbon atom),carboxyl group amide group,amine group,nucleotide others others aromatic ring (only carbon atom),carboxyl group amide group,amine group,nucleotide H2O
ChEBI 16238
30763
16474
15379
26689
27140
15378
36062
18009
15377
PubChem 643975
135
3702506
5884
977
1038
72
5886
22247451
962
1bf3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1bgjA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1bgnA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1bkwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1cc4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1cc6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1cj2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1cj3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1cj4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1d7lA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:RFL Unbound Unbound Unbound Unbound Unbound
1dobA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1docA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1dodA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1doeA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1iusA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1iutA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1iuuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1iuvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1iuwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1iuxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1pbbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1pbcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1pbdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1pbeA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1pbfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1pdhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:FAS Unbound Unbound Unbound Unbound Unbound
1phhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1pxaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1pxbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1pxcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
2phhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:APR Unbound Unbound Unbound Unbound Unbound
1bf3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1bgjA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1bgnA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1bkwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1cc4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1cc6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1cj2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1cj3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1cj4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1d7lA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1dobA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1docA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1dodA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:DOB Unbound
1doeA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:DOB Unbound
1iusA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PAB Unbound Unbound Unbound Unbound
1iutA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PAB Unbound Unbound Unbound Unbound
1iuuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PAB Unbound Unbound Unbound Unbound
1iuvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1iuwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1iuxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1pbbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:DOB Unbound
1pbcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:BHA Unbound
1pbdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PAB Unbound Unbound Unbound Unbound
1pbeA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1pbfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:BHA Unbound
1pdhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1phhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Bound:DHB Unbound
1pxaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1pxbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
1pxcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound
2phhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:PHB Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1cc4, 1cc6 & literature [12]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bf3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant R42K, C116S
1bgjA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant C116S, H162R
1bgnA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant C116S
1bkwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant R44K, C116S
1cc4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant C116S, F161A
1cc6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant C116S, R166S
1cj2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant Q34R
1cj3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant Y38E
1cj4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant Q34T
1d7lA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1dobA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1docA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1dodA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1doeA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iusA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iutA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iuuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iuvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iuwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iuxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pbbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant C116S
1pbcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant C116S
1pbdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant C116S
1pbeA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pbfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant C116S
1pdhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1phhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pxaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant N300D
1pxbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pxcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2phhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bf3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385 invisible Y385
1bgjA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1bgnA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385 mutant R269T
1bkwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1cc4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1cc6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1cj2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1cj3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1cj4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1d7lA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1dobA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385 mutant Y222F
1docA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1dodA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1doeA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1iusA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1iutA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1iuuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1iuvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1iuwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1iuxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1pbbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1pbcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1pbdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1pbeA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1pbfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385 mutant Y222A
1pdhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1phhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1pxaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385
1pxbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;TYR 385 mutant Y201F
1pxcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201; mutant Y385F
2phhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 201;TYR 385

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.72-73
[4]
Fig.3, Fig.4
[5]
Fig.3
[7]
Fig.1, p.647
[10]
Fig.1, Fig.2, Fig.6, Fig.7, Fig.8, p.3104-3106
[12]
p.144-145
[13]
Fig.1
[14]
Scheme 1
[16]
Fig.1
[18]
Scheme 1, Scheme 2, Scheme 3, p.574-578
[24]
Fig.1, Scheme 1, p.6294-6298
[25]
Scheme 1, p.16641-16646
[30]
Fig.1, p.170-172
[33]
Scheme 2, Scheme 7
[36]
Fig.1
[37]
Fig.1, p.22212-22215
[38]
Fig.1, p.1573-1579
[39]
Fig.1
[40]
Fig.1, p.305-309

References
[1]
Resource
Comments
Medline ID
PubMed ID 807574
Journal J Biol Chem
Year 1975
Volume 250
Pages 5268-9
Authors Drenth J, Hol WG, Wierenga RK
Title Crystallization and preliminary x-ray investigation of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 819305
Journal FEBS Lett
Year 1976
Volume 65
Pages 84-6
Authors Marius A, Schepman, Schutter WG, van Bruggen EF
Title Electron microscopic studies on microcrystals of parahydroxybenzoate hydroxylase from Pseudomonas fluorescens.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 80029705
PubMed ID 40036
Journal J Mol Biol
Year 1979
Volume 131
Pages 55-73
Authors Wierenga RK, de Jong RJ, Kalk KH, Hol WG, Drenth J
Title Crystal structure of p-hydroxybenzoate hydroxylase.
Related PDB
Related UniProtKB P00438
[4]
Resource
Comments
Medline ID
PubMed ID 6617648
Journal Eur J Biochem
Year 1983
Volume 135
Pages 543-8
Authors Visser CM
Title Reaction mechanism of flavin-dependent hydroxylation. Evolution of a non-imitable enzyme.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 6235473
Journal Orig Life
Year 1984
Volume 14
Pages 699-705
Authors Visser CM
Title Evolution of biocatalysis 4. Nicotinamide, flavin and dioxygen dependent hydroxylation. Origin of a non-imitable enzyme.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 3343242
Journal J Biol Chem
Year 1988
Volume 263
Pages 3131-6
Authors Schreuder HA, Hol WG, Drenth J
Title Molecular modeling reveals the possible importance of a carbonyl oxygen binding pocket for the catalytic mechanism of p-hydroxybenzoate hydroxylase.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID 88172509
PubMed ID 3351945
Journal J Mol Biol
Year 1988
Volume 199
Pages 637-48
Authors Schreuder HA, van der Laan JM, Hol WG, Drenth J
Title Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate.
Related PDB 1phh
Related UniProtKB P00438
[8]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2819062
Journal Biochemistry
Year 1989
Volume 28
Pages 7199-205
Authors van der Laan JM, Schreuder HA, Swarte MB, Wierenga RK, Kalk KH, Hol WG, Drenth J
Title The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation.
Related PDB 2phh
Related UniProtKB
[9]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2553983
Journal J Mol Biol
Year 1989
Volume 208
Pages 679-96
Authors Schreuder HA, Prick PA, Wierenga RK, Vriend G, Wilson KS, Hol WG, Drenth J
Title Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes.
Related PDB 1pbe
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 2337581
Journal Biochemistry
Year 1990
Volume 29
Pages 3101-8
Authors Schreuder HA, Hol WG, Drenth J
Title Analysis of the active site of the flavoprotein p-hydroxybenzoate hydroxylase and some ideas with respect to its reaction mechanism.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF REDUCED FORM
Medline ID 93028353
PubMed ID 1409567
Journal Proteins
Year 1992
Volume 14
Pages 178-90
Authors Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J
Title Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution.
Related PDB
Related UniProtKB P00438
[12]
Resource
Comments
Medline ID
PubMed ID 8365400
Journal Eur J Biochem
Year 1993
Volume 216
Pages 137-46
Authors Eschrich K, van der Bolt FJ, de Kok A, van Berkel WJ
Title Role of Tyr201 and Tyr385 in substrate activation by p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS
Medline ID 94146010
PubMed ID 8312276
Journal Biochemistry
Year 1994
Volume 33
Pages 1555-64
Authors Lah MS, Palfey BA, Schreuder HA, Ludwig ML
Title Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.
Related PDB 1pxa 1pxb 1pxc
Related UniProtKB P20586
[13]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7520279
Journal Biochemistry
Year 1994
Volume 33
Pages 10161-70
Authors Schreuder HA, Mattevi A, Obmolova G, Kalk KH, Hol WG, van der Bolt FJ, van Berkel WJ
Title Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring.
Related PDB 1pbb 1pbc 1pbd 1pbf
Related UniProtKB
[15]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7756982
Journal Protein Sci
Year 1994
Volume 3
Pages 2245-53
Authors van Berkel WJ, Eppink MH, Schreuder HA
Title Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin.
Related PDB 1pdh
Related UniProtKB
[16]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 95025875
PubMed ID 7939628
Journal Science
Year 1994
Volume 266
Pages 110-4
Authors Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML
Title The mobile flavin of 4-OH benzoate hydroxylase.
Related PDB 1dob 1doc 1dod 1doe
Related UniProtKB P20586
[17]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-44
Medline ID 95354684
PubMed ID 7628466
Journal Eur J Biochem
Year 1995
Volume 231
Pages 157-65
Authors Eppink MH, Schreuder HA, Van Berkel WJ
Title Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding.
Related PDB 1bkw
Related UniProtKB P00438
[18]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 96140232
PubMed ID 8555229
Journal Biochemistry
Year 1996
Volume 35
Pages 567-78
Authors Gatti DL, Entsch B, Ballou DP, Ludwig ML
Title pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis.
Related PDB 1ius 1iut 1iuu 1iuv 1iuw 1iux
Related UniProtKB P20586
[19]
Resource
Comments
Medline ID
PubMed ID 9369493
Journal Biochemistry
Year 1997
Volume 36
Pages 14192-201
Authors van der Bolt FJ, van den Heuvel RH, Vervoort J, van Berkel WJ
Title 19F NMR study on the regiospecificity of hydroxylation of tetrafluoro-4-hydroxybenzoate by wild-type and Y385F p-hydroxybenzoate hydroxylase: evidence for a consecutive oxygenolytic dehalogenation mechanism.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 9385648
Journal Protein Sci
Year 1997
Volume 6
Pages 2454-8
Authors Eppink MH, Schreuder HA, Van Berkel WJ
Title Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 9546198
Journal Biophys Chem
Year 1998
Volume 70
Pages 217-22
Authors Mattevi A
Title The PHBH fold: not only flavoenzymes.
Related PDB
Related UniProtKB
[22]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-42 AND SER-42
Medline ID 98237589
PubMed ID 9578477
Journal Eur J Biochem
Year 1998
Volume 253
Pages 194-201
Authors Eppink MH, Schreuder HA, van Berkel WJ
Title Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding.
Related PDB 1bf3
Related UniProtKB P00438
[23]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9694855
Journal J Biol Chem
Year 1998
Volume 273
Pages 21031-9
Authors Eppink MH, Schreuder HA, van Berkel WJ
Title Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants.
Related PDB 1bgj 1bgn
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 10320359
Journal Biochemistry
Year 1999
Volume 38
Pages 6292-9
Authors Moran GR, Entsch B, Palfey BA, Ballou DP
Title Mechanistic insights into p-hydroxybenzoate hydroxylase from studies of the mutant Ser212Ala.
Related PDB
Related UniProtKB
[25]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10600126
Journal Biochemistry
Year 1999
Volume 38
Pages 16636-47
Authors Ortiz-Maldonado M, Gatti D, Ballou DP, Massey V
Title Structure-function correlations of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins.
Related PDB 1d7l
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 9930974
Journal Biochemistry
Year 1999
Volume 38
Pages 1153-8
Authors Palfey BA, Moran GR, Entsch B, Ballou DP, Massey V
Title Substrate recognition by "password" in p-hydroxybenzoate hydroxylase.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 10606503
Journal Biochemistry
Year 1999
Volume 38
Pages 16727-32
Authors Zheng Y, Dong J, Palfey BA, Carey PR
Title Using Raman spectroscopy to monitor the solvent-exposed and "buried" forms of flavin in p-hydroxybenzoate hydroxylase.
Related PDB
Related UniProtKB
[28]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF VARIANTS
Medline ID 99148809
PubMed ID 10025942
Journal FEBS Lett
Year 1999
Volume 443
Pages 251-5
Authors Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ
Title Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.
Related PDB 1cc4 1cc6
Related UniProtKB P00438
[29]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10493859
Journal J Mol Biol
Year 1999
Volume 292
Pages 87-96
Authors Eppink MH, Overkamp KM, Schreuder HA, Van Berkel WJ
Title Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase.
Related PDB 1cj2 1cj3 1cj4
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 10736773
Journal J Mol Graph Model
Year 1999
Volume 17
Pages 163-75, 214
Authors Ridder L, Mulholland AJ, Rietjens IM, Vervoort J
Title Combined quantum mechanical and molecular mechanical reaction pathway calculation for aromatic hydroxylation by p-hydroxybenzoate-3-hydroxylase.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 10922496
Journal FEBS Lett
Year 2000
Volume 478
Pages 197-201
Authors Ridder L, Palfey BA, Vervoort J, Rietjens IM
Title Modelling flavin and substrate substituent effects on the activation barrier and rate of oxygen transfer by p-hydroxybenzoate hydroxylase.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 11300768
Journal Biochemistry
Year 2001
Volume 40
Pages 3891-9
Authors Frederick KK, Ballou DP, Palfey BA
Title Protein dynamics control proton transfers to the substrate on the His72Asn mutant of p-hydroxybenzoate hydroxylase.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 11170433
Journal Biochemistry
Year 2001
Volume 40
Pages 1091-101
Authors Ortiz-Maldonado M, Ballou DP, Massey V
Title A rate-limiting conformational change of the flavin in p-hydroxybenzoate hydroxylase is necessary for ligand exchange and catalysis: studies with 8-mercapto- and 8-hydroxy-flavins.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 11248022
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 3006-11
Authors Altose MD, Zheng Y, Dong J, Palfey BA, Carey PR
Title Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 11805318
Journal Proc Natl Acad Sci U S A
Year 2002
Volume 99
Pages 608-13
Authors Wang J, Ortiz-Maldonado M, Entsch B, Massey V, Ballou D, Gatti DL
Title Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 14503873
Journal Biochemistry
Year 2003
Volume 42
Pages 11234-42
Authors Ortiz-Maldonado M, Entsch B, Ballou DP
Title Conformational changes combined with charge-transfer interactions are essential for reduction in catalysis by p-hydroxybenzoate hydroxylase.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 12684497
Journal J Biol Chem
Year 2003
Volume 278
Pages 22210-6
Authors Palfey BA, Murthy YV, Massey V
Title Altered balance of half-reactions in p-hydroxybenzoate hydroxylase caused by substituting the 2'-carbon of FAD with fluorine.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 14769033
Journal Biochemistry
Year 2004
Volume 43
Pages 1569-79
Authors Ortiz-Maldonado M, Cole LJ, Dumas SM, Entsch B, Ballou DP
Title Increased positive electrostatic potential in p-hydroxybenzoate hydroxylase accelerates hydroxylation but slows turnover.
Related PDB
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 14709077
Journal J Am Chem Soc
Year 2004
Volume 126
Pages 127-42
Authors Bach RD, Dmitrenko O
Title Model studies on p-hydroxybenzoate hydroxylase. The catalytic role of Arg-214 and Tyr-201 in the hydroxylation step.
Related PDB
Related UniProtKB
[40]
Resource
Comments
Medline ID
PubMed ID 15581585
Journal Arch Biochem Biophys
Year 2005
Volume 433
Pages 297-311
Authors Entsch B, Cole LJ, Ballou DP
Title Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.
Related PDB
Related UniProtKB

Comments
According to the literature [10], [13], [14] & [40], this enzyme catalyzes the following reactions:
(A) Hydride transfer from NADPH to FAD, forming FADH2 (Reduction of FAD by NADPH) (Reductive half-reaction):
(B) Oxygenation of hydroxybenzoate by O2 at FADH2 (Oxidative half-reaction):
(B1) Oxygenation to form a flavin 4a-hydroperoxide intermediate.
(B2) Additive double-bond deformation; Addition of hydroxyl group to substrate, 4-hydroxybenzoate, by flavin 4a-hydroperoxide intermediate (Hydroxylation of substrate), forming 3,4-dihydroxybenzoate and a flavin 4a-hydroxide intermediate.
(B3) Eliminative double-bond formation; Elimination of H2O from flavin 4a-hydroxide intermediate, giving FAD.

Created Updated
2004-03-24 2009-02-26