Sequence of PHHY_PSEFL
EC Number:1.14.13.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
Other sequences found for EC No. 1.14.13.2
General information:
Sequence
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 Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
333545
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
333546
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
333547
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
333548
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
333549
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
333550
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
333551
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
333552
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
333553
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
333554
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
333555
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
333556
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
333557
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
333558
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
333559
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
333560
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
333561
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
333562
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
