BRENDA - Enzyme Database show
show all sequences of 1.14.14.20

Gene redundancy of two-component (chloro)phenol hydroxylases in Rhodococcus opacus 1CP

Groening, J.; Eulberg, D.; Tischler, D.; Kaschabek, S.; Schloemann, M.; FEMS Microbiol. Lett. 361, 68-75 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
genes pheA1(1-3), phylogenetic analysis, typical for genes of the peripheral degradation of aromatic compounds, pheA1(13) and pheA2(1-3) are not located within gene clusters for central ortho- and meta-cleavage pathway. All three gene sets are nearby to genes with function in (chloro)aromatic degradation
Rhodococcus opacus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
290000
310000
isozymes, gel filtration
Rhodococcus opacus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2,4-dichlorophenol + FADH2 + O2
Rhodococcus opacus
-
2,4-dichlorocatechol + FAD + H2O
-
-
?
2,4-dichlorophenol + FADH2 + O2
Rhodococcus opacus 1CP
-
2,4-dichlorocatechol + FAD + H2O
-
-
?
2-chlorophenol + FADH2 + O2
Rhodococcus opacus
poor substrate for isozyme PheA1(1)
2-chlorocatechol + FAD + H2O
-
-
?
2-chlorophenol + FADH2 + O2
Rhodococcus opacus 1CP
poor substrate for isozyme PheA1(1)
2-chlorocatechol + FAD + H2O
-
-
?
4-chlorophenol + FADH2 + O2
Rhodococcus opacus
-
4-chlorocatechol + FAD + H2O
-
-
?
4-chlorophenol + FADH2 + O2
Rhodococcus opacus 1CP
-
4-chlorocatechol + FAD + H2O
-
-
?
4-methylphenol + FADH2 + O2
Rhodococcus opacus
-
4-methylcatechol + FAD + H2O
-
-
?
additional information
Rhodococcus opacus
substrate speccificities of the three isozymes, overview
?
-
-
-
additional information
Rhodococcus opacus 1CP
substrate speccificities of the three isozymes, overview
?
-
-
-
phenol + FADH2 + O2
Rhodococcus opacus
-
catechol + FAD + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodococcus opacus
A0A069AW73
gene pheA1(1); gene pheA1(1)
-
Rhodococcus opacus 1CP
A0A069AW73
gene pheA1(1); gene pheA1(1)
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,4-dichlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus
2,4-dichlorocatechol + FAD + H2O
-
-
-
?
2,4-dichlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus 1CP
2,4-dichlorocatechol + FAD + H2O
-
-
-
?
2-chlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus
2-chlorocatechol + FAD + H2O
-
-
-
?
2-chlorophenol + FADH2 + O2
poor substrate for isozyme PheA1(1)
736121
Rhodococcus opacus
2-chlorocatechol + FAD + H2O
-
-
-
?
2-chlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus 1CP
2-chlorocatechol + FAD + H2O
-
-
-
?
2-chlorophenol + FADH2 + O2
poor substrate for isozyme PheA1(1)
736121
Rhodococcus opacus 1CP
2-chlorocatechol + FAD + H2O
-
-
-
?
4-chlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus
4-chlorocatechol + FAD + H2O
-
-
-
?
4-chlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus 1CP
4-chlorocatechol + FAD + H2O
-
-
-
?
4-methylphenol + FADH2 + O2
-
736121
Rhodococcus opacus
4-methylcatechol + FAD + H2O
-
-
-
?
additional information
substrate speccificities of the three isozymes, overview
736121
Rhodococcus opacus
?
-
-
-
-
additional information
substrate speccificities of the three isozymes, overview
736121
Rhodococcus opacus 1CP
?
-
-
-
-
phenol + FADH2 + O2
-
736121
Rhodococcus opacus
catechol + FAD + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
oligomer
homotetrameric or homohexameric structure, all phenol hydroxylase isoenzymes, x * 59000-63000, SDS-PAGE
Rhodococcus opacus
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Rhodococcus opacus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Rhodococcus opacus
Cofactor
Cofactor
Commentary
Organism
Structure
FADH2
FAD is again reduced at the expense of NADH and NADPH
Rhodococcus opacus
Cloned(Commentary) (protein specific)
Commentary
Organism
genes pheA1(1-3), phylogenetic analysis, typical for genes of the peripheral degradation of aromatic compounds, pheA1(13) and pheA2(1-3) are not located within gene clusters for central ortho- and meta-cleavage pathway. All three gene sets are nearby to genes with function in (chloro)aromatic degradation
Rhodococcus opacus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FADH2
FAD is again reduced at the expense of NADH and NADPH
Rhodococcus opacus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
290000
310000
isozymes, gel filtration
Rhodococcus opacus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2,4-dichlorophenol + FADH2 + O2
Rhodococcus opacus
-
2,4-dichlorocatechol + FAD + H2O
-
-
?
2,4-dichlorophenol + FADH2 + O2
Rhodococcus opacus 1CP
-
2,4-dichlorocatechol + FAD + H2O
-
-
?
2-chlorophenol + FADH2 + O2
Rhodococcus opacus
poor substrate for isozyme PheA1(1)
2-chlorocatechol + FAD + H2O
-
-
?
2-chlorophenol + FADH2 + O2
Rhodococcus opacus 1CP
poor substrate for isozyme PheA1(1)
2-chlorocatechol + FAD + H2O
-
-
?
4-chlorophenol + FADH2 + O2
Rhodococcus opacus
-
4-chlorocatechol + FAD + H2O
-
-
?
4-chlorophenol + FADH2 + O2
Rhodococcus opacus 1CP
-
4-chlorocatechol + FAD + H2O
-
-
?
4-methylphenol + FADH2 + O2
Rhodococcus opacus
-
4-methylcatechol + FAD + H2O
-
-
?
additional information
Rhodococcus opacus
substrate speccificities of the three isozymes, overview
?
-
-
-
additional information
Rhodococcus opacus 1CP
substrate speccificities of the three isozymes, overview
?
-
-
-
phenol + FADH2 + O2
Rhodococcus opacus
-
catechol + FAD + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,4-dichlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus
2,4-dichlorocatechol + FAD + H2O
-
-
-
?
2,4-dichlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus 1CP
2,4-dichlorocatechol + FAD + H2O
-
-
-
?
2-chlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus
2-chlorocatechol + FAD + H2O
-
-
-
?
2-chlorophenol + FADH2 + O2
poor substrate for isozyme PheA1(1)
736121
Rhodococcus opacus
2-chlorocatechol + FAD + H2O
-
-
-
?
2-chlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus 1CP
2-chlorocatechol + FAD + H2O
-
-
-
?
2-chlorophenol + FADH2 + O2
poor substrate for isozyme PheA1(1)
736121
Rhodococcus opacus 1CP
2-chlorocatechol + FAD + H2O
-
-
-
?
4-chlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus
4-chlorocatechol + FAD + H2O
-
-
-
?
4-chlorophenol + FADH2 + O2
-
736121
Rhodococcus opacus 1CP
4-chlorocatechol + FAD + H2O
-
-
-
?
4-methylphenol + FADH2 + O2
-
736121
Rhodococcus opacus
4-methylcatechol + FAD + H2O
-
-
-
?
additional information
substrate speccificities of the three isozymes, overview
736121
Rhodococcus opacus
?
-
-
-
-
additional information
substrate speccificities of the three isozymes, overview
736121
Rhodococcus opacus 1CP
?
-
-
-
-
phenol + FADH2 + O2
-
736121
Rhodococcus opacus
catechol + FAD + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
oligomer
homotetrameric or homohexameric structure, all phenol hydroxylase isoenzymes, x * 59000-63000, SDS-PAGE
Rhodococcus opacus
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Rhodococcus opacus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Rhodococcus opacus
General Information
General Information
Commentary
Organism
evolution
phylogenetic analysis shows exceptional high similarities of PheA1(1-3) and PheA2(1-3) to putative phenol hydroxylases in several Rhodococcus strains, overview
Rhodococcus opacus
General Information (protein specific)
General Information
Commentary
Organism
evolution
phylogenetic analysis shows exceptional high similarities of PheA1(1-3) and PheA2(1-3) to putative phenol hydroxylases in several Rhodococcus strains, overview
Rhodococcus opacus
Other publictions for EC 1.14.14.20
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
735546
Szoekoel
Induction and carbon catabolit ...
Rhodococcus erythropolis, Rhodococcus erythropolis CCM2595, Rhodococcus jostii
Appl. Microbiol. Biotechnol.
98
8267-8279
2014
-
-
2
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
2
2
3
-
-
736121
Groening
Gene redundancy of two-compone ...
Rhodococcus opacus 1CP, Rhodococcus opacus
FEMS Microbiol. Lett.
361
68-75
2014
-
-
1
-
-
-
-
-
-
-
1
10
-
2
-
-
-
-
-
-
-
-
12
1
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
10
-
-
-
-
-
-
-
-
12
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
736132
Orenes-Pinero
A new process for obtaining hy ...
Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius A7
Food Chem.
139
377-383
2013
-
1
1
-
1
-
-
-
-
-
2
2
-
11
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
1
-
-
-
-
2
2
1
-
2
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
2
4
-
-
-
-
-
-
-
-
-
1
2
-
-
-
701875
Saa
Cloning, purification and char ...
Rhodococcus erythropolis, Rhodococcus erythropolis UPV-1
Appl. Microbiol. Biotechnol.
86
201-211
2009
1
1
1
-
-
-
12
6
-
2
9
2
-
6
-
-
1
-
-
1
2
-
24
2
2
-
-
-
1
-
-
6
-
2
-
1
2
2
10
-
-
-
-
13
-
6
-
2
9
2
-
-
-
2
-
2
2
-
24
2
3
-
-
-
2
-
-
2
-
1
2
-
-
-
691504
Omokoko
Isolation of the phe-operon fr ...
Geobacillus stearothermophilus
BMC Microbiol.
8
197
2008
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
736400
van den Heuvel
Structural studies on flavin r ...
Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius A7
J. Biol. Chem.
279
12860-12867
2004
-
-
1
1
-
-
-
-
-
-
-
2
-
4
-
-
1
1
-
-
-
-
4
1
1
-
-
-
1
-
-
3
-
-
-
-
-
1
3
1
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
4
1
1
-
-
-
1
-
-
-
-
2
2
-
-
-
659279
Kirchner
Phenol hydroxylase from Bacill ...
Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius A7
J. Biol. Chem.
278
47545-47553
2003
2
-
1
-
-
-
-
4
-
-
4
6
-
15
-
-
1
-
-
-
3
4
16
2
2
1
5
3
3
1
-
6
-
3
-
2
-
3
7
-
-
-
-
-
-
4
-
-
5
6
-
-
-
3
-
-
4
4
16
2
3
1
8
3
3
1
-
5
-
2
3
-
3
3
736171
Duffner
Phenol/cresol degradation by t ...
Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius A7
Gene
256
215-221
2000
-
-
1
-
-
-
-
-
1
-
2
4
-
13
-
-
-
-
-
-
-
-
4
1
-
-
-
-
-
-
-
1
-
-
-
-
-
2
2
-
-
-
-
-
-
-
2
-
2
4
-
-
-
-
-
-
-
-
4
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
438788
Straube
Phenol hydroxylase from Rhodoc ...
Rhodococcus sp., Rhodococcus sp. P1
J. Basic Microbiol.
27
229-232
1987
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
21
-
1
1
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
21
-
1
1
-
-
1
-
-
-
-
-
-
-
-
-