BRENDA - Enzyme Database

Biochemical properties of ectoine hydroxylases from extremophiles and their wider taxonomic distribution among microorganisms

Widderich, N.; Hoeppner, A.; Pittelkow, M.; Heider, J.; Smits, S.H.; Bremer, E.; PLoS ONE 9, e93809 (2014)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization (Commentary)
Organism
1.14.11.55
to 1.9 A resolution, and comparison of iron-bound and apo structure. The iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Virgibacillus salexigens
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.14.11.55
NaCl
maximum activity in presence of 50 mM KCl. High concentrations of NaCl are inhibitory
Acidiphilium cryptum
1.14.11.55
NaCl
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
Alkalilimnicola ehrlichii
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Halomonas elongata
1.14.11.55
NaCl
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
Paenibacillus lautus
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Pseudomonas stutzeri
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Sphingopyxis alaskensis
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Virgibacillus salexigens
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.14.11.55
2.7
-
2-oxoglutarate
pH 7.5, 32C
Sphingopyxis alaskensis
1.14.11.55
3.9
-
2-oxoglutarate
pH 7.5, 32C
Paenibacillus lautus
1.14.11.55
4.1
-
2-oxoglutarate
pH 7.5, 32C
Acidiphilium cryptum
1.14.11.55
4.6
-
2-oxoglutarate
pH 7.5, 32C
Pseudomonas stutzeri
1.14.11.55
4.8
-
2-oxoglutarate
pH 7.5, 32C
Halomonas elongata
1.14.11.55
4.9
-
2-oxoglutarate
pH 7.5, 32C
Virgibacillus salexigens
1.14.11.55
5
-
2-oxoglutarate
pH 7.5, 32C
Alkalilimnicola ehrlichii
1.14.11.55
5.7
-
ectoine
pH 7.5, 32C
Halomonas elongata
1.14.11.55
5.9
-
ectoine
pH 7.5, 32C
Virgibacillus salexigens
1.14.11.55
6.2
-
ectoine
pH 7.5, 32C
Pseudomonas stutzeri
1.14.11.55
9
-
ectoine
pH 7.5, 32C
Alkalilimnicola ehrlichii
1.14.11.55
9.5
-
ectoine
pH 7.5, 32C
Paenibacillus lautus
1.14.11.55
9.8
-
ectoine
pH 7.5, 32C
Sphingopyxis alaskensis
1.14.11.55
10
-
ectoine
pH 7.5, 32C
Acidiphilium cryptum
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Acidiphilium cryptum
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Alkalilimnicola ehrlichii
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Halomonas elongata
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Paenibacillus lautus
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Pseudomonas stutzeri
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Sphingopyxis alaskensis
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Virgibacillus salexigens
1.14.11.55
KCl
maximum activity in presence of 100 mM KCl
Acidiphilium cryptum
1.14.11.55
KCl
maximum activity in presence of 150 mM KCl
Alkalilimnicola ehrlichii
1.14.11.55
KCl
maximum activity in presence of 150 mM KCl
Halomonas elongata
1.14.11.55
KCl
maximum activity in presence of 200 mM KCl
Paenibacillus lautus
1.14.11.55
KCl
maximum activity in presence of 150 mM KCl
Pseudomonas stutzeri
1.14.11.55
KCl
maximum activity in presence of 100 mM KCl
Sphingopyxis alaskensis
1.14.11.55
KCl
maximum activity in presence of 150 mM KCl
Virgibacillus salexigens
1.14.11.55
NaCl
maximum activity in presence of 50 mM KCl. High concentrations of NaCl are inhibitory
Acidiphilium cryptum
1.14.11.55
NaCl
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
Alkalilimnicola ehrlichii
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Halomonas elongata
1.14.11.55
NaCl
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
Paenibacillus lautus
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Pseudomonas stutzeri
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Sphingopyxis alaskensis
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Virgibacillus salexigens
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.14.11.55
34100
-
-
Acidiphilium cryptum
1.14.11.55
34100
-
-
Sphingopyxis alaskensis
1.14.11.55
34200
-
x * 34200, SDS-PAGE
Pseudomonas stutzeri
1.14.11.55
34300
-
x * 34300, SDS-PAGE
Alkalilimnicola ehrlichii
1.14.11.55
34400
-
x * 34400, SDS-PAGE
Virgibacillus salexigens
1.14.11.55
34800
-
x * 34800, SDS-PAGE
Paenibacillus lautus
1.14.11.55
37400
-
-
Halomonas elongata
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.14.11.55
ectoine + 2-oxoglutarate + O2
Pseudomonas stutzeri
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Virgibacillus salexigens
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Sphingopyxis alaskensis
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Halomonas elongata
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Paenibacillus lautus
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Alkalilimnicola ehrlichii
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Acidiphilium cryptum
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Pseudomonas stutzeri A1501
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Sphingopyxis alaskensis DSM 13593
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Halomonas elongata DSM 2581
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
additional information
Pseudomonas stutzeri
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Virgibacillus salexigens
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Sphingopyxis alaskensis
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Halomonas elongata
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Paenibacillus lautus
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Alkalilimnicola ehrlichii
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Acidiphilium cryptum
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Pseudomonas stutzeri A1501
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Sphingopyxis alaskensis DSM 13593
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Halomonas elongata DSM 2581
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.14.11.55
Acidiphilium cryptum
JN019030
ectD gene optimized for the expression in Escherichia coli
-
1.14.11.55
Alkalilimnicola ehrlichii
JN019031
ectD gene optimized for the expression in Escherichia coli
-
1.14.11.55
Halomonas elongata
E1VA04
-
-
1.14.11.55
Halomonas elongata DSM 2581
E1VA04
-
-
1.14.11.55
Paenibacillus lautus
A0A1R1AUM9
ectD gene optimized for the expression in Escherichia coli
-
1.14.11.55
Pseudomonas stutzeri
-
-
-
1.14.11.55
Pseudomonas stutzeri A1501
-
-
-
1.14.11.55
Sphingopyxis alaskensis
Q1GNW5
-
-
1.14.11.55
Sphingopyxis alaskensis DSM 13593
Q1GNW5
-
-
1.14.11.55
Virgibacillus salexigens
Q2TDY4
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Pseudomonas stutzeri
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Virgibacillus salexigens
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Sphingopyxis alaskensis
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Halomonas elongata
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Paenibacillus lautus
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Alkalilimnicola ehrlichii
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Acidiphilium cryptum
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Pseudomonas stutzeri A1501
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Sphingopyxis alaskensis DSM 13593
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Halomonas elongata DSM 2581
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Pseudomonas stutzeri
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Virgibacillus salexigens
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Sphingopyxis alaskensis
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Halomonas elongata
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Paenibacillus lautus
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Alkalilimnicola ehrlichii
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Acidiphilium cryptum
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Pseudomonas stutzeri A1501
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Sphingopyxis alaskensis DSM 13593
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Halomonas elongata DSM 2581
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
1.14.11.55
?
x * 34100, SDS-PAGE
Acidiphilium cryptum
1.14.11.55
?
x * 34300, SDS-PAGE
Alkalilimnicola ehrlichii
1.14.11.55
?
x * 37400, SDS-PAGE
Halomonas elongata
1.14.11.55
?
x * 34800, SDS-PAGE
Paenibacillus lautus
1.14.11.55
?
x * 34200, SDS-PAGE
Pseudomonas stutzeri
1.14.11.55
?
x * 34100, SDS-PAGE
Sphingopyxis alaskensis
1.14.11.55
?
x * 34400, SDS-PAGE
Virgibacillus salexigens
Synonyms
EC Number
Synonyms
Commentary
Organism
1.14.11.55
ectD
-
Acidiphilium cryptum
1.14.11.55
ectD
-
Alkalilimnicola ehrlichii
1.14.11.55
ectD
-
Halomonas elongata
1.14.11.55
ectD
-
Paenibacillus lautus
1.14.11.55
ectD
-
Pseudomonas stutzeri
1.14.11.55
ectD
-
Sphingopyxis alaskensis
1.14.11.55
ectD
-
Virgibacillus salexigens
1.14.11.55
Sala_2952
-
Sphingopyxis alaskensis
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
1.14.11.55
32
-
-
Acidiphilium cryptum
1.14.11.55
32
-
-
Halomonas elongata
1.14.11.55
32
-
-
Virgibacillus salexigens
1.14.11.55
35
-
-
Alkalilimnicola ehrlichii
1.14.11.55
35
-
-
Pseudomonas stutzeri
1.14.11.55
40
-
-
Paenibacillus lautus
1.14.11.55
40
-
-
Sphingopyxis alaskensis
Temperature Range [C]
EC Number
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
1.14.11.55
5
47
-
Halomonas elongata
1.14.11.55
5
50
-
Sphingopyxis alaskensis
1.14.11.55
5
50
-
Virgibacillus salexigens
1.14.11.55
10
47
-
Acidiphilium cryptum
1.14.11.55
10
50
-
Pseudomonas stutzeri
1.14.11.55
15
45
-
Alkalilimnicola ehrlichii
1.14.11.55
15
50
-
Paenibacillus lautus
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.14.11.55
1.2
-
ectoine
pH 7.5, 32C
Alkalilimnicola ehrlichii
1.14.11.55
1.2
-
ectoine
pH 7.5, 32C
Sphingopyxis alaskensis
1.14.11.55
1.6
-
ectoine
pH 7.5, 32C
Paenibacillus lautus
1.14.11.55
2.8
-
ectoine
pH 7.5, 32C
Halomonas elongata
1.14.11.55
3.4
-
ectoine
pH 7.5, 32C
Acidiphilium cryptum
1.14.11.55
7.7
-
ectoine
pH 7.5, 32C
Virgibacillus salexigens
1.14.11.55
8.9
-
ectoine
pH 7.5, 32C
Pseudomonas stutzeri
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.14.11.55
7.5
-
-
Alkalilimnicola ehrlichii
1.14.11.55
7.5
-
-
Paenibacillus lautus
1.14.11.55
7.5
-
-
Pseudomonas stutzeri
1.14.11.55
7.5
-
-
Virgibacillus salexigens
1.14.11.55
8
-
-
Acidiphilium cryptum
1.14.11.55
8
-
-
Halomonas elongata
1.14.11.55
8
-
-
Sphingopyxis alaskensis
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.14.11.55
5.5
9.6
-
Acidiphilium cryptum
1.14.11.55
5.5
9.6
-
Paenibacillus lautus
1.14.11.55
5.5
9.6
-
Pseudomonas stutzeri
1.14.11.55
5.5
9.6
-
Sphingopyxis alaskensis
1.14.11.55
5.5
9.6
-
Virgibacillus salexigens
1.14.11.55
6.5
9.6
-
Alkalilimnicola ehrlichii
1.14.11.55
6.5
9.6
-
Halomonas elongata
pI Value
EC Number
Organism
Commentary
pI Value Maximum
pI Value
1.14.11.55
Pseudomonas stutzeri
calculated
-
5.5
1.14.11.55
Sphingopyxis alaskensis
calculated
-
5.5
1.14.11.55
Paenibacillus lautus
calculated
-
5.6
1.14.11.55
Alkalilimnicola ehrlichii
calculated
-
5.7
1.14.11.55
Acidiphilium cryptum
calculated
-
5.8
1.14.11.55
Halomonas elongata
calculated
-
5.8
1.14.11.55
Virgibacillus salexigens
calculated
-
5.8
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.14.11.55
to 1.9 A resolution, and comparison of iron-bound and apo structure. The iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Virgibacillus salexigens
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.14.11.55
NaCl
maximum activity in presence of 50 mM KCl. High concentrations of NaCl are inhibitory
Acidiphilium cryptum
1.14.11.55
NaCl
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
Alkalilimnicola ehrlichii
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Halomonas elongata
1.14.11.55
NaCl
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
Paenibacillus lautus
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Pseudomonas stutzeri
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Sphingopyxis alaskensis
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Virgibacillus salexigens
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.14.11.55
2.7
-
2-oxoglutarate
pH 7.5, 32C
Sphingopyxis alaskensis
1.14.11.55
3.9
-
2-oxoglutarate
pH 7.5, 32C
Paenibacillus lautus
1.14.11.55
4.1
-
2-oxoglutarate
pH 7.5, 32C
Acidiphilium cryptum
1.14.11.55
4.6
-
2-oxoglutarate
pH 7.5, 32C
Pseudomonas stutzeri
1.14.11.55
4.8
-
2-oxoglutarate
pH 7.5, 32C
Halomonas elongata
1.14.11.55
4.9
-
2-oxoglutarate
pH 7.5, 32C
Virgibacillus salexigens
1.14.11.55
5
-
2-oxoglutarate
pH 7.5, 32C
Alkalilimnicola ehrlichii
1.14.11.55
5.7
-
ectoine
pH 7.5, 32C
Halomonas elongata
1.14.11.55
5.9
-
ectoine
pH 7.5, 32C
Virgibacillus salexigens
1.14.11.55
6.2
-
ectoine
pH 7.5, 32C
Pseudomonas stutzeri
1.14.11.55
9
-
ectoine
pH 7.5, 32C
Alkalilimnicola ehrlichii
1.14.11.55
9.5
-
ectoine
pH 7.5, 32C
Paenibacillus lautus
1.14.11.55
9.8
-
ectoine
pH 7.5, 32C
Sphingopyxis alaskensis
1.14.11.55
10
-
ectoine
pH 7.5, 32C
Acidiphilium cryptum
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Acidiphilium cryptum
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Alkalilimnicola ehrlichii
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Halomonas elongata
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Paenibacillus lautus
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Pseudomonas stutzeri
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Sphingopyxis alaskensis
1.14.11.55
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EH motif, the so-called 2-His-1-carboxylate facial triad
Virgibacillus salexigens
1.14.11.55
KCl
maximum activity in presence of 100 mM KCl
Acidiphilium cryptum
1.14.11.55
KCl
maximum activity in presence of 150 mM KCl
Alkalilimnicola ehrlichii
1.14.11.55
KCl
maximum activity in presence of 150 mM KCl
Halomonas elongata
1.14.11.55
KCl
maximum activity in presence of 200 mM KCl
Paenibacillus lautus
1.14.11.55
KCl
maximum activity in presence of 150 mM KCl
Pseudomonas stutzeri
1.14.11.55
KCl
maximum activity in presence of 100 mM KCl
Sphingopyxis alaskensis
1.14.11.55
KCl
maximum activity in presence of 150 mM KCl
Virgibacillus salexigens
1.14.11.55
NaCl
maximum activity in presence of 50 mM KCl. High concentrations of NaCl are inhibitory
Acidiphilium cryptum
1.14.11.55
NaCl
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
Alkalilimnicola ehrlichii
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Halomonas elongata
1.14.11.55
NaCl
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
Paenibacillus lautus
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Pseudomonas stutzeri
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Sphingopyxis alaskensis
1.14.11.55
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
Virgibacillus salexigens
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.14.11.55
34100
-
-
Acidiphilium cryptum
1.14.11.55
34100
-
-
Sphingopyxis alaskensis
1.14.11.55
34200
-
x * 34200, SDS-PAGE
Pseudomonas stutzeri
1.14.11.55
34300
-
x * 34300, SDS-PAGE
Alkalilimnicola ehrlichii
1.14.11.55
34400
-
x * 34400, SDS-PAGE
Virgibacillus salexigens
1.14.11.55
34800
-
x * 34800, SDS-PAGE
Paenibacillus lautus
1.14.11.55
37400
-
-
Halomonas elongata
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.14.11.55
ectoine + 2-oxoglutarate + O2
Pseudomonas stutzeri
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Virgibacillus salexigens
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Sphingopyxis alaskensis
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Halomonas elongata
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Paenibacillus lautus
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Alkalilimnicola ehrlichii
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Acidiphilium cryptum
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Pseudomonas stutzeri A1501
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Sphingopyxis alaskensis DSM 13593
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
Halomonas elongata DSM 2581
-
5-hydroxyectoine + succinate + CO2
-
-
ir
1.14.11.55
additional information
Pseudomonas stutzeri
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Virgibacillus salexigens
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Sphingopyxis alaskensis
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Halomonas elongata
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Paenibacillus lautus
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Alkalilimnicola ehrlichii
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Acidiphilium cryptum
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Pseudomonas stutzeri A1501
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Sphingopyxis alaskensis DSM 13593
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
1.14.11.55
additional information
Halomonas elongata DSM 2581
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
?
-
-
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Pseudomonas stutzeri
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Virgibacillus salexigens
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Sphingopyxis alaskensis
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Halomonas elongata
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Paenibacillus lautus
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Alkalilimnicola ehrlichii
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Acidiphilium cryptum
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Pseudomonas stutzeri A1501
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Sphingopyxis alaskensis DSM 13593
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
ectoine + 2-oxoglutarate + O2
-
741304
Halomonas elongata DSM 2581
5-hydroxyectoine + succinate + CO2
-
-
-
ir
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Pseudomonas stutzeri
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Virgibacillus salexigens
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Sphingopyxis alaskensis
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Halomonas elongata
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Paenibacillus lautus
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Alkalilimnicola ehrlichii
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Acidiphilium cryptum
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Pseudomonas stutzeri A1501
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Sphingopyxis alaskensis DSM 13593
?
-
-
-
-
1.14.11.55
additional information
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
741304
Halomonas elongata DSM 2581
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.14.11.55
?
x * 34100, SDS-PAGE
Acidiphilium cryptum
1.14.11.55
?
x * 34300, SDS-PAGE
Alkalilimnicola ehrlichii
1.14.11.55
?
x * 37400, SDS-PAGE
Halomonas elongata
1.14.11.55
?
x * 34800, SDS-PAGE
Paenibacillus lautus
1.14.11.55
?
x * 34200, SDS-PAGE
Pseudomonas stutzeri
1.14.11.55
?
x * 34100, SDS-PAGE
Sphingopyxis alaskensis
1.14.11.55
?
x * 34400, SDS-PAGE
Virgibacillus salexigens
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
1.14.11.55
32
-
-
Acidiphilium cryptum
1.14.11.55
32
-
-
Halomonas elongata
1.14.11.55
32
-
-
Virgibacillus salexigens
1.14.11.55
35
-
-
Alkalilimnicola ehrlichii
1.14.11.55
35
-
-
Pseudomonas stutzeri
1.14.11.55
40
-
-
Paenibacillus lautus
1.14.11.55
40
-
-
Sphingopyxis alaskensis
Temperature Range [C] (protein specific)
EC Number
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
1.14.11.55
5
47
-
Halomonas elongata
1.14.11.55
5
50
-
Sphingopyxis alaskensis
1.14.11.55
5
50
-
Virgibacillus salexigens
1.14.11.55
10
47
-
Acidiphilium cryptum
1.14.11.55
10
50
-
Pseudomonas stutzeri
1.14.11.55
15
45
-
Alkalilimnicola ehrlichii
1.14.11.55
15
50
-
Paenibacillus lautus
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.14.11.55
1.2
-
ectoine
pH 7.5, 32C
Alkalilimnicola ehrlichii
1.14.11.55
1.2
-
ectoine
pH 7.5, 32C
Sphingopyxis alaskensis
1.14.11.55
1.6
-
ectoine
pH 7.5, 32C
Paenibacillus lautus
1.14.11.55
2.8
-
ectoine
pH 7.5, 32C
Halomonas elongata
1.14.11.55
3.4
-
ectoine
pH 7.5, 32C
Acidiphilium cryptum
1.14.11.55
7.7
-
ectoine
pH 7.5, 32C
Virgibacillus salexigens
1.14.11.55
8.9
-
ectoine
pH 7.5, 32C
Pseudomonas stutzeri
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.14.11.55
7.5
-
-
Alkalilimnicola ehrlichii
1.14.11.55
7.5
-
-
Paenibacillus lautus
1.14.11.55
7.5
-
-
Pseudomonas stutzeri
1.14.11.55
7.5
-
-
Virgibacillus salexigens
1.14.11.55
8
-
-
Acidiphilium cryptum
1.14.11.55
8
-
-
Halomonas elongata
1.14.11.55
8
-
-
Sphingopyxis alaskensis
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.14.11.55
5.5
9.6
-
Acidiphilium cryptum
1.14.11.55
5.5
9.6
-
Paenibacillus lautus
1.14.11.55
5.5
9.6
-
Pseudomonas stutzeri
1.14.11.55
5.5
9.6
-
Sphingopyxis alaskensis
1.14.11.55
5.5
9.6
-
Virgibacillus salexigens
1.14.11.55
6.5
9.6
-
Alkalilimnicola ehrlichii
1.14.11.55
6.5
9.6
-
Halomonas elongata
pI Value (protein specific)
EC Number
Organism
Commentary
pI Value Maximum
pI Value
1.14.11.55
Pseudomonas stutzeri
calculated
-
5.5
1.14.11.55
Sphingopyxis alaskensis
calculated
-
5.5
1.14.11.55
Paenibacillus lautus
calculated
-
5.6
1.14.11.55
Alkalilimnicola ehrlichii
calculated
-
5.7
1.14.11.55
Acidiphilium cryptum
calculated
-
5.8
1.14.11.55
Halomonas elongata
calculated
-
5.8
1.14.11.55
Virgibacillus salexigens
calculated
-
5.8
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.14.11.55
0.12
-
ectoine
pH 7.5, 32C
Sphingopyxis alaskensis
1.14.11.55
0.13
-
ectoine
pH 7.5, 32C
Alkalilimnicola ehrlichii
1.14.11.55
0.17
-
ectoine
pH 7.5, 32C
Paenibacillus lautus
1.14.11.55
0.34
-
ectoine
pH 7.5, 32C
Acidiphilium cryptum
1.14.11.55
0.49
-
ectoine
pH 7.5, 32C
Halomonas elongata
1.14.11.55
1.31
-
ectoine
pH 7.5, 32C
Virgibacillus salexigens
1.14.11.55
1.44
-
ectoine
pH 7.5, 32C
Pseudomonas stutzeri
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.14.11.55
0.12
-
ectoine
pH 7.5, 32C
Sphingopyxis alaskensis
1.14.11.55
0.13
-
ectoine
pH 7.5, 32C
Alkalilimnicola ehrlichii
1.14.11.55
0.17
-
ectoine
pH 7.5, 32C
Paenibacillus lautus
1.14.11.55
0.34
-
ectoine
pH 7.5, 32C
Acidiphilium cryptum
1.14.11.55
0.49
-
ectoine
pH 7.5, 32C
Halomonas elongata
1.14.11.55
1.31
-
ectoine
pH 7.5, 32C
Virgibacillus salexigens
1.14.11.55
1.44
-
ectoine
pH 7.5, 32C
Pseudomonas stutzeri