p-hydroxybenzoate hydroxylase

Namep-hydroxybenzoate hydroxylase
Synonyms
  • 1.14.13.2
  • 4-hydroxybenzoate 3-monooxygenase
Gene NamepobA
OrganismPseudomonas fluorescens
Amino acid sequence
>lcl|BSEQ0016465|p-hydroxybenzoate hydroxylase
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAG
VDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATT
VYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERV
YPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW
TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN
LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFS
QRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
Number of residues394
Molecular Weight44321.205
Theoretical pI6.8
GO Classification
Functions
  • FAD binding
  • 4-hydroxybenzoate 3-monooxygenase activity
Processes
  • benzoate catabolic process via hydroxylation
General FunctionFad binding
Specific FunctionNot Available
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID49145
UniProtKB IDP00438
UniProtKB Entry NamePHHY_PSEFL
Cellular LocationNot Available
Gene sequence
>lcl|BSEQ0003023|1185 bp
ATGAAGACTCAAGTCGCCATCATCGGCGCCGGTCCGTCCGGCCTCCTGCTCGGCCAGTTG
CTGCACAAGGCCGGCATCGACAACGTGATCCTCGAACGCCAGACCCCGGACTACGTGCTC
GGCCGCATCCGCGCCGGCGTGCTGGAACAGGGTATGGTCGACCTGCTGCGCGAGGCCGGC
GTCGACCGGCGCATGGCGCGCGACGGGCTGGTCCACGAAGGCGTGGAGATCGCCTTCGCC
GGGCAGCGCCGGCGCATCGACCTGAAGCGCCTGAGCGGCGGCAAGACGGTGACGGTCTAC
GGCCAGACCGAGGTCACCCGCGACCTCATGGAAGCCCGCGAAGCCTGCGGCGCCACTACC
GTCTACCAGGCCGCCGAGGTGCGCCTGCACGACCTGCAAGGTGAGCGCCCCTACGTGACC
TTCGAACGCGACGGCGAACGGCTACGCCTGGATTGCGACTACATCGCCGGCTGCGATGGC
TTCCACGGCATCTCGCGGCAATCGATCCCGGCGGAGCGGCTGAAGGTCTTCGAGCGGGTC
TATCCGTTCGGCTGGCTCGGCCTGCTCGCCGACACCCCGCCGGTCAGCCACGAACTGATC
TACGCCAACCATCCGCGCGGCTTCGCCCTGTGCAGCCAGCGTTCGGCGACCCGCAGCCGC
TACTACGTACAGGTGCCATTGACAGAGAAGGTCGAGGACTGGTCCGACGAGCGCTTCTGG
ACGGAACTGAAAGCGCGCCTCCCGGCCGAGGTGGCGGAGAAACTGGTGACCGGTCCTTCG
CTGGAGAAGAGCATCGCGCCGCTGCGCAGCTTCGTGGTCGAGCCGATGCAGCATGGCCGG
CTGTTCCTCGCCGGCGACGCCGCGCACATCGTGCCGCCCACCGGCGCCAAGGGACTGAAC
CTGGCGGCCAGCGACGTCAGCACGCTCTACCGGCTGCTGCTGAAGGCCTACCGCGAAGGG
CGGGGCGAACTGCTGGAACGCTACTCGGCAATCTGCCTGCGGCGGATCTGGAAGGCCGAA
CGCTTCTCCTGGTGGATGACTTCGGTGCTGCATCGCTTCCCCGACACCGACGCGTTCAGC
CAGCGCATCCAGCAGACCGAACTGGAGTACTACCTGGGCTCCGAGGCGGGCCTGGCGACC
ATCGCCGAGAACTATGTCGGCCTGCCCTACGAGGAAATCGAGTAG
GenBank Gene IDX68438
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
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. 1459126
  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. 6809053
  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. 6780352
  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. 6780353
  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. 6406229
  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. 6406227
  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. 40036
  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. 3351945
  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. 1409567
  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. 7628466
  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. 9578477
  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. 10025942