Sequence of PHHY_PSEFL

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
4-hydroxybenzoate 3-monooxygenase
P00438
Pseudomonas fluorescens
394
44322
Reaction
4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
Sequences with same EC No.
Sequence
show sequence in fasta format
  0 MKTQVAIIGA GPSGLLLGQL LHKAGIDNVI LERQTPDYVL GRIRAGVLEQ GMVDLLREAG
 60 VDRRMARDGL VHEGVEIAFA GQRRRIDLKR LSGGKTVTVY GQTEVTRDLM EAREACGATT
120 VYQAAEVRLH DLQGERPYVT FERDGERLRL DCDYIAGCDG FHGISRQSIP AERLKVFERV
180 YPFGWLGLLA DTPPVSHELI YANHPRGFAL CSQRSATRSR YYVQVPLTEK VEDWSDERFW
240 TELKARLPAE VAEKLVTGPS LEKSIAPLRS FVVEPMQHGR LFLAGDAAHI VPPTGAKGLN
300 LAASDVSTLY RLLLKAYREG RGELLERYSA ICLRRIWKAE RFSWWMTSVL HRFPDTDAFS
360 QRIQQTELEY YLGSEAGLAT IAENYVGLPY EEIE
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
199123
van Berkel W.,Westphal A.,Eschrich K.,Eppink M.,de Kok A.
Substitution of Arg214 at the substrate-binding site of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
Eur. J. Biochem.
210
411-419
1992
199124
Weijer W.J.,Hofsteenge J.,Vereijken J.M.,Jekel P.A.,Beintema J.J.
Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
Biochim. Biophys. Acta
704
385-388
1982
199125
Hofsteenge J.,Vereijken J.M.,Weijer W.J.,Beintema J.J.,Wierenga R.K.,Drenth J.
Primary and tertiary structure studies of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Isolation and alignment of the CNBr peptides; interactions of the protein with flavin adenine dinucleotide.
Eur. J. Biochem.
113
141-150
1980
199126
Vereijken J.M.,Hofsteenge J.,Bak H.J.,Beintema J.J.
The amino-acid sequence of the three smallest CNBr peptides from p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
Eur. J. Biochem.
113
151-157
1980
199127
Hofsteenge J.,Weijer W.J.,Jekel P.A.,Beintema J.J.
p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 1. Completion of the elucidation of the primary structure.
Eur. J. Biochem.
133
91-108
1983
199128
Weijer W.J.,Hofsteenge J.,Beintema J.J.,Wierenga R.K.,Drenth J.
p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure.
Eur. J. Biochem.
133
109-118
1983
199129
Wierenga R.K.,de Jong R.J.,Kalk K.H.,Hol W.G.J.,Drenth J.
Crystal structure of p-hydroxybenzoate hydroxylase.
J. Mol. Biol.
131
55-73
1979
199130
Schreuder H.A.,van der Laan J.M.,Swarte M.B.A.,Kalk K.H.,Hol W.G.J.,Drenth J.
Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3-A resolution.
Proteins
14
178-190
1992
199131
Schreuder H.A.,van der Laan J.M.,Hol W.G.,Drenth J.
Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate.
J. Mol. Biol.
199
637-648
1988
199132
van der Laan J.M.,Schreuder H.A.,Swarte M.B.,Wierenga R.K.,Kalk K.H.,Hol W.G.,Drenth J.
The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation.
Biochemistry
28
7199-7205
1989
199133
Schreuder H.A.,Prick P.A.,Wierenga R.K.,Vriend G.,Wilson K.S.,Hol W.G.,Drenth J.
Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes.
J. Mol. Biol.
208
679-696
1989
199134
Schreuder H.A.,Mattevi A.,Obmolova G.,Kalk K.H.,Hol W.G.,van der Bolt F.J.,van Berkel W.J.
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.
Biochemistry
33
10161-10170
1994
199135
van Berkel W.J.,Eppink M.H.,Schreuder H.A.
Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin.
Protein Sci.
3
2245-2253
1994
199136
Eppink M.H.,Schreuder H.A.,Van Berkel W.J.
Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding.
Eur. J. Biochem.
231
157-165
1995
199137
Eppink M.H.,Schreuder H.A.,van Berkel W.J.
Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding.
Eur. J. Biochem.
253
194-201
1998
199138
Eppink M.H.,Schreuder H.A.,van Berkel W.J.
Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants.
J. Biol. Chem.
273
21031-21039
1998
199139
Eppink M.H.,Bunthol C.,Schreuder H.A.,van Berkel W.J.
Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.
FEBS Lett.
443
251-255
1999
199140
Eppink M.H.,Overkamp K.M.,Schreuder H.A.,Van Berkel W.J.
Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase.
J. Mol. Biol.
292
87-96
1999