p-hydroxybenzoate hydroxylase
Details
- Name
- p-hydroxybenzoate hydroxylase
- Synonyms
- 1.14.13.2
- 4-hydroxybenzoate 3-monooxygenase
- Gene Name
- pobA
- Organism
- Pseudomonas fluorescens
- Amino acid sequence
>lcl|BSEQ0016465|p-hydroxybenzoate hydroxylase MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAG VDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATT VYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERV YPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFS QRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
- Number of residues
- 394
- Molecular Weight
- 44321.205
- Theoretical pI
- 6.8
- GO Classification
- Functions4-hydroxybenzoate 3-monooxygenase activity / FAD bindingProcessesbenzoate catabolic process via hydroxylation
- General Function
- Fad binding
- Specific Function
- Not Available
- Pfam Domain Function
- FAD_binding_3 (PF01494)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not 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
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00438 UniProtKB Entry Name PHHY_PSEFL GenBank Protein ID 49145 GenBank Gene ID X68438 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02059 Adenosine-5-Diphosphoribose experimental unknown Details DB02839 2,4-Dihydroxybenzoic Acid experimental unknown Details DB03147 Flavin adenine dinucleotide approved unknown Details DB04242 4-hydroxybenzoic acid experimental unknown Details DB02362 Aminobenzoic acid approved, experimental unknown substrate Details