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P-hydroxybenzoate hydroxylase

ID 2769
Name P-hydroxybenzoate hydroxylase
Synonyms
  • EC 1.14.13.2
  • 4-hydroxybenzoate 3- monooxygenase
Gene Name pobA
Protein Sequence 
>P-hydroxybenzoate hydroxylase
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAG
VDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATT
VYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERV
YPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW
TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN
LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFS
QRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
Number of Residues 394
Molecular Weight 44322
Theoretical pI 6.80
GO Classification
Function
catalytic activity
oxidoreductase activity
monooxygenase activity
Process
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
aromatic compound metabolism
General Function Coenzyme transport and metabolism
Specific Function 4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O
Pathways Not Available
Reactions
  • 4-hydroxybenzoate + NADPH + H+ + O2 = protocatechuate + NADP+ + H2O
Pfam Domain Function
Signals None
Transmembrane Regions None
Essentiality Non-Essential
GenBank Protein ID 49145 Link_out
UniProtKB ID P00438 Link_out
UniProtKB Entry Name PHHY_PSEFL Link_out
PDB ID 2PHH Link_out
PDB File show
3D Structure View 3D Structure
Cellular Location Not Available
Gene Sequence 
>1185 bp
ATGAAGACTCAAGTCGCCATCATCGGCGCCGGTCCGTCCGGCCTCCTGCTCGGCCAGTTG
CTGCACAAGGCCGGCATCGACAACGTGATCCTCGAACGCCAGACCCCGGACTACGTGCTC
GGCCGCATCCGCGCCGGCGTGCTGGAACAGGGTATGGTCGACCTGCTGCGCGAGGCCGGC
GTCGACCGGCGCATGGCGCGCGACGGGCTGGTCCACGAAGGCGTGGAGATCGCCTTCGCC
GGGCAGCGCCGGCGCATCGACCTGAAGCGCCTGAGCGGCGGCAAGACGGTGACGGTCTAC
GGCCAGACCGAGGTCACCCGCGACCTCATGGAAGCCCGCGAAGCCTGCGGCGCCACTACC
GTCTACCAGGCCGCCGAGGTGCGCCTGCACGACCTGCAAGGTGAGCGCCCCTACGTGACC
TTCGAACGCGACGGCGAACGGCTACGCCTGGATTGCGACTACATCGCCGGCTGCGATGGC
TTCCACGGCATCTCGCGGCAATCGATCCCGGCGGAGCGGCTGAAGGTCTTCGAGCGGGTC
TATCCGTTCGGCTGGCTCGGCCTGCTCGCCGACACCCCGCCGGTCAGCCACGAACTGATC
TACGCCAACCATCCGCGCGGCTTCGCCCTGTGCAGCCAGCGTTCGGCGACCCGCAGCCGC
TACTACGTACAGGTGCCATTGACAGAGAAGGTCGAGGACTGGTCCGACGAGCGCTTCTGG
ACGGAACTGAAAGCGCGCCTCCCGGCCGAGGTGGCGGAGAAACTGGTGACCGGTCCTTCG
CTGGAGAAGAGCATCGCGCCGCTGCGCAGCTTCGTGGTCGAGCCGATGCAGCATGGCCGG
CTGTTCCTCGCCGGCGACGCCGCGCACATCGTGCCGCCCACCGGCGCCAAGGGACTGAAC
CTGGCGGCCAGCGACGTCAGCACGCTCTACCGGCTGCTGCTGAAGGCCTACCGCGAAGGG
CGGGGCGAACTGCTGGAACGCTACTCGGCAATCTGCCTGCGGCGGATCTGGAAGGCCGAA
CGCTTCTCCTGGTGGATGACTTCGGTGCTGCATCGCTTCCCCGACACCGACGCGTTCAGC
CAGCGCATCCAGCAGACCGAACTGGAGTACTACCTGGGCTCCGAGGCGGGCCTGGCGACC
ATCGCCGAGAACTATGTCGGCCTGCCCTACGAGGAAATCGAGTAG
GenBank Gene ID X68438 Link_out
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
HPRD ID Not Available
IUPHAR ID Not Available
Guide to Pharmacology ID Not Available
Chromosome Location Not Available
Locus Not Available
SNPs pobA Link_out
General References
  1. 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. 1992 Dec 1;210(2):411-9. Pubmed
  2. Weijer WJ, Hofsteenge J, Vereijken JM, Jekel PA, Beintema JJ: Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Biochim Biophys Acta. 1982 Jun 4;704(2):385-8. Pubmed
  3. Hofsteenge J, Vereijken JM, Weijer WJ, Beintema JJ, Wierenga RK, 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. 1980 Dec;113(1):141-50. Pubmed
  4. Vereijken JM, Hofsteenge J, Bak HJ, Beintema JJ: The amino-acid sequence of the three smallest CNBr peptides from p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Eur J Biochem. 1980 Dec;113(1):151-7. Pubmed
  5. Hofsteenge J, Weijer WJ, Jekel PA, Beintema JJ: p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 1. Completion of the elucidation of the primary structure. Eur J Biochem. 1983 Jun 1;133(1):91-108. Pubmed
  6. Weijer WJ, Hofsteenge J, Beintema JJ, Wierenga RK, Drenth J: p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure. Eur J Biochem. 1983 Jun 1;133(1):109-18. Pubmed
  7. Wierenga RK, de Jong RJ, Kalk KH, Hol WG, Drenth J: Crystal structure of p-hydroxybenzoate hydroxylase. J Mol Biol. 1979 Jun 15;131(1):55-73. Pubmed
  8. Schreuder HA, van der Laan JM, Hol WG, Drenth J: Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate. J Mol Biol. 1988 Feb 20;199(4):637-48. Pubmed
  9. Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J: Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution. Proteins. 1992 Oct;14(2):178-90. Pubmed
  10. Eppink MH, Schreuder HA, Van Berkel WJ: Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding. Eur J Biochem. 1995 Jul 1;231(1):157-65. Pubmed
  11. Eppink MH, Schreuder HA, van Berkel WJ: Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding. Eur J Biochem. 1998 Apr 1;253(1):194-201. Pubmed
  12. Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ: Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability. FEBS Lett. 1999 Jan 29;443(3):251-5. Pubmed
Drugs
# DrugBank ID Drug Name Drug Type Drug Groups
1 DB02839 2,4-Dihydroxybenzoic Acid small molecule experimental
2 DB02362 4-Aminobenzoic Acid small molecule experimental
3 DB02059 Adenosine-5-Diphosphoribose small molecule experimental
4 DB03147 Flavin-Adenine Dinucleotide small molecule experimental
5 DB04242 P-Hydroxybenzoic Acid small molecule experimental