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D-fructose 6-phosphate + H2O
?
-
-
-
-
?
L-histidinol 1-phosphate + H2O
L-histidinol + phosphate
105% of the activity with D-myo-inositol1-phosphate
-
-
?
L-histidinol phosphate + H2O
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
L-phosphoserine + H2O
L-serine + phosphate
-
-
-
-
?
N-formyl-L-histidinol phosphate + H2O
N-formyl-L-histidinol + phosphate
additional information
?
-
L-histidinol phosphate + H2O
?
-
-
-
-
?
L-histidinol phosphate + H2O
?
-
-
-
-
?
L-histidinol phosphate + H2O
?
-
-
-
-
?
L-histidinol phosphate + H2O
?
-
-
-
-
?
L-histidinol phosphate + H2O
?
-
-
-
-
?
L-histidinol phosphate + H2O
?
-
-
-
-
?
L-histidinol phosphate + H2O
?
-
-
-
-
?
L-histidinol phosphate + H2O
?
-
-
-
-
?
L-histidinol phosphate + H2O
?
-
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
low activity
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
low activity
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
low activity
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
low activity
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
low activity
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
low activity
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
the enzyme catalyses the eigthth step of histidine biosynthesis
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
the enzyme catalyses the eigthth step of histidine biosynthesis
-
?
N-formyl-L-histidinol phosphate + H2O
N-formyl-L-histidinol + phosphate
the rate of hydrolysis of N-formyl-L-histidinol phosphate is less than 1% of the rate of hydrolysis of L-histidinol phosphate at pH 8.5
-
-
?
N-formyl-L-histidinol phosphate + H2O
N-formyl-L-histidinol + phosphate
the rate of hydrolysis of N-formyl-L-histidinol phosphate is less than 1% of the rate of hydrolysis of L-histidinol phosphate at pH 8.5
-
-
?
additional information
?
-
-
no substrate: 4-nitrophenyl phosphate
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate
-
-
?
additional information
?
-
-
no substrate: 4-nitrophenyl phosphate
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate
-
-
?
additional information
?
-
no activity with inositol monophosphate by wild-type or mutant Mtb HolPases. Phosphate detection with malachite green
-
-
?
additional information
?
-
-
no activity with inositol monophosphate by wild-type or mutant Mtb HolPases. Phosphate detection with malachite green
-
-
?
additional information
?
-
no activity with inositol monophosphate by wild-type or mutant Mtb HolPases. Phosphate detection with malachite green
-
-
?
additional information
?
-
no activity with inositol monophosphate by wild-type or mutant Mtb HolPases. Phosphate detection with malachite green
-
-
?
additional information
?
-
-
does not show any phosphatase activity with p-nitrophenyl phosphate
-
-
?
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Be2+
-
increases Km at pH 6.5
Cu2+
-
strong activity in the presence of Cu2+
Iron
contains iron in the active site
Co2+
20% of the activity with Mg2+
Co2+
20% activation compared to Mg2+ at 5 mM
Co2+
47% of the activity with Mg2+
Co2+
50% activation compared to Mg2+ at 5 mM
Co2+
-
shifts optimal pH to 6.5, decreases Km at pH 6.5
Co2+
-
strong activity in the presence of Co2+
Fe2+
-
decreases Km at pH 6.5
Fe2+
-
part of the trinuclear metal center
Mg2+
assay in presence of 2 mM
Mg2+
activates, best divalent cation
Mg2+
assay in presence of 5 mM, Km value 0.65 mM, Hill coefficient 2.44
Mg2+
required for activity, best at 5 mM
Mg2+
a divalent cation is required, saturation kinetics for Mtb HolPase with Mg2+ as a cofactor, the specificity constant (kcat/Km) with Zn2+ is 1.16fold higher compared to Mg2+, metal binding in the active site of Mtb HolPase, structure, overview
Mg2+
-
shifts optimal pH to 6.5
Mg2+
-
strong activity in the presence of Mg2+
Mn2+
11% of the activity with Mg2+
Mn2+
78% of the activity with Mg2+
Mn2+
10% activation compared to Mg2+ at 5 mM
Mn2+
75-80% activation compared to Mg2+ at 5 mM
Mn2+
-
shifts optimal pH to 6.5, decreases Km at pH 6.5
Mn2+
-
strong activity in the presence of Mn2+
Ni2+
-
increases Km at pH 6.5
Ni2+
-
strong activity in the presence of Ni2+
Zn2+
-
activating
Zn2+
-
the presence of a structural Zn2+ ion stabilizes the conformation of an extended loop
Zn2+
contains Zn2+ in the active site
Zn2+
a divalent cation is required, saturation kinetics for Mtb HolPase with Zn2+ as a cofactor, the specificity constant (kcat/Km) with Zn2+ is 1.16fold higher compared to Mg2+, Michaelis-Menten kinetics, overview
Zn2+
-
shifts optimal pH to 6.5, decreases Km at pH 6.5
Zn2+
-
part of the trinuclear metal center
additional information
-
divalent cation is required
additional information
divalent cation is required
additional information
divalent cation is required
additional information
-
no activating effect by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
no activating effect by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
no activating effect by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
-
no activating effect on activity by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
no activating effect on activity by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
no activating effect on activity by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
the enzyme does not show any significant increases in catalytic activity when Zn2+, Mn2+, Co2+ or Ni2+ are added
additional information
-
the enzyme does not show any significant increases in catalytic activity when Zn2+, Mn2+, Co2+ or Ni2+ are added
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0.59
AMP
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
2.37
D-fructose 6-phosphate
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
0.18
L-histidinol 1-phosphate
pH 7.5, 25°C
0.0236 - 5.4
L-histidinol phosphate
1.45
L-phosphoserine
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
additional information
additional information
-
0.0236
L-histidinol phosphate
pH 7.4, 30°C, Hill coefficient 1.47
0.03
L-histidinol phosphate
-
in the presence of Mn2+, at 80°C and pH 6.5
0.03198
L-histidinol phosphate
pH 8.0, 37°C, recombinant enzyme
0.041
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Zn2+
0.05
L-histidinol phosphate
-
in the presence of Co2+, at 80°C and pH 6.5
0.052
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mn2+
0.054
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Co2+
0.054
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mg2+
0.09
L-histidinol phosphate
-
in the presence of Mg2+, at 80°C and pH 6.5
0.09
L-histidinol phosphate
-
in the presence of Ni2+, at 80°C and pH 6.5
0.1 - 0.3
L-histidinol phosphate
-
-
0.11
L-histidinol phosphate
-
-
0.13
L-histidinol phosphate
-
-
0.14
L-histidinol phosphate
mutant enzyme D228N, at pH 9.0 and 22°C
0.15
L-histidinol phosphate
-
-
0.25
L-histidinol phosphate
-
-
0.263
L-histidinol phosphate
pH 8.4, 22°C
0.27
L-histidinol phosphate
-
-
0.3
L-histidinol phosphate
-
-
0.638
L-histidinol phosphate
pH 7.4, 30°C, Hill coefficient 1.47
0.74
L-histidinol phosphate
mutant enzyme Y117F, at pH 9.0 and 22°C
1.3
L-histidinol phosphate
mutant enzyme H42N, at pH 9.0 and 22°C
1.5
L-histidinol phosphate
mutant enzyme R160M, at pH 9.0 and 22°C
1.7
L-histidinol phosphate
mutant enzyme E115Q, at pH 9.0 and 22°C
1.7
L-histidinol phosphate
mutant enzyme HY157F, at pH 9.0 and 22°C
1.9
L-histidinol phosphate
wild type enzyme, at pH 9.0 and 22°C
2.3
L-histidinol phosphate
mutant enzyme Y161F, at pH 9.0 and 22°C
2.5
L-histidinol phosphate
mutant enzyme Y161A, at pH 9.0 and 22°C
4.2
L-histidinol phosphate
-
-
4.5
L-histidinol phosphate
mutant enzyme R197M, at pH 9.0 and 22°C
5.4
L-histidinol phosphate
mutant enzyme Y117A, at pH 9.0 and 22°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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29
AMP
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
11
D-fructose 6-phosphate
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
1.3
L-histidinol 1-phosphate
pH 7.5, 25°C
0.013 - 2140
L-histidinol phosphate
14
L-phosphoserine
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
0.013
L-histidinol phosphate
pH 7.4, 30°C
0.031
L-histidinol phosphate
mutant enzyme D228N, at pH 9.0 and 22°C
0.62
L-histidinol phosphate
mutant enzyme H42N, at pH 9.0 and 22°C
0.74
L-histidinol phosphate
mutant enzyme R160M, at pH 9.0 and 22°C
0.93
L-histidinol phosphate
-
-
0.99
L-histidinol phosphate
pH 8.0, 37°C, recombinant enzyme
1.04
L-histidinol phosphate
pH 7.4, 30°C
3.6
L-histidinol phosphate
pH 8.4, 22°C
20 - 50
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Co2+
31
L-histidinol phosphate
mutant enzyme E115Q, at pH 9.0 and 22°C
38
L-histidinol phosphate
mutant enzyme R197M, at pH 9.0 and 22°C
48
L-histidinol phosphate
mutant enzyme Y161A, at pH 9.0 and 22°C
53
L-histidinol phosphate
mutant enzyme Y117A, at pH 9.0 and 22°C
61
L-histidinol phosphate
mutant enzyme HY157F, at pH 9.0 and 22°C
110
L-histidinol phosphate
mutant enzyme Y117F, at pH 9.0 and 22°C
174
L-histidinol phosphate
wild type enzyme, at pH 9.0 and 22°C
180
L-histidinol phosphate
mutant enzyme Y161F, at pH 9.0 and 22°C
260
L-histidinol phosphate
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
290
L-histidinol phosphate
-
in the presence of 1 mM Ni2+, at 80°C and pH 6.5
320
L-histidinol phosphate
-
in the presence of 1 mM Mn2+, at 80°C and pH 6.5
420
L-histidinol phosphate
-
in the presence of 1 mM Mg2+, at 80°C and pH 6.5
960
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mn2+
1410
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Zn2+
2140
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mg2+
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evolution
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
evolution
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
evolution
enzyme Mtb HolPase belongs to the IMPase family, it is not an active inositol monophosphate phosphatase (IMPase) but a histidinol phosphate phosphatase (HolPase)
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
enzyme Mtb HolPase belongs to the IMPase family, it is not an active inositol monophosphate phosphatase (IMPase) but a histidinol phosphate phosphatase (HolPase)
-
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
enzyme Mtb HolPase belongs to the IMPase family, it is not an active inositol monophosphate phosphatase (IMPase) but a histidinol phosphate phosphatase (HolPase)
-
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
malfunction
deletion of the histidinol-phosphate phosphatase gene hisN results in histidine auxotrophy
malfunction
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
physiological function
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
physiological function
IMPase-like HPPs play a role only in His biosynthesis
physiological function
the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
physiological function
-
the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
-
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
physiological function
-
the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
-
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
additional information
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
additional information
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
additional information
the cocrystal structure of Mtb HolPase with HOLP reveals a unique mode of substrate binding, a multizinc active-site pocket, and a product-exit channel. Dephosphorylation mechanism of Mtb Hol-Pase, overview
additional information
-
the cocrystal structure of Mtb HolPase with HOLP reveals a unique mode of substrate binding, a multizinc active-site pocket, and a product-exit channel. Dephosphorylation mechanism of Mtb Hol-Pase, overview
additional information
the histidinol phosphate dephosphorylation reaction occurs at the interface between N- and C-terminal domains, structure-function relationship, active site structure with bound substrate, overview
additional information
-
the histidinol phosphate dephosphorylation reaction occurs at the interface between N- and C-terminal domains, structure-function relationship, active site structure with bound substrate, overview
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
additional information
-
the cocrystal structure of Mtb HolPase with HOLP reveals a unique mode of substrate binding, a multizinc active-site pocket, and a product-exit channel. Dephosphorylation mechanism of Mtb Hol-Pase, overview
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
additional information
-
the cocrystal structure of Mtb HolPase with HOLP reveals a unique mode of substrate binding, a multizinc active-site pocket, and a product-exit channel. Dephosphorylation mechanism of Mtb Hol-Pase, overview
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
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monomer
-
1 * 39000, gel filtration
?
x * 60000, SDS-PAGE, recombinant GST-fusion protein
?
-
x * 16000-18000, SDS-PAGE
?
-
x * 16000-18000, SDS-PAGE
-
dimer
-
2 * 19903, in the presence of Mg2+ and histidinol phosphate, ESI mass spectrometry
dimer
2 * 30378, recombinant enzyme, mass spectrometry, the monomer is with the N-terminal SNA linker that resides after cleavage with tobacco etch virus protease, plus the difference from the two added methylene groups (24 Da) with SNAMSS adduct (577.6 Da) that most probably is an artifact resulting from the MS experiment
dimer
2 * 28620, recombinant enzyme, SDS-PAGE
dimer
-
2 * 28620, recombinant enzyme, SDS-PAGE
-
dimer
-
2 * 28620, recombinant enzyme, SDS-PAGE
-
homotetramer
-
4 * 29976
homotetramer
-
4 * 29500, dynamic light scattering
homotetramer
-
4 * 29976, calculated from sequence of cDNA
homotetramer
-
4 * 29500, dynamic light scattering
-
homotetramer
-
4 * 29976, calculated from sequence of cDNA
-
homotetramer
-
4 * 29976
-
additional information
covalent dimerization of MtHPP, a monomer of MtHPP has an alphabetaalphabetaalpha-sandwich-like arrangement. The N-terminal domain, which forms an alpha + beta structure, covers residues from the N-terminus to Glu201. Two long alpha-helices (alpha1 and alpha2) are separated by a mobile loop. The eight-stranded beta-sheet of the N-terminal domain contains a alpha-loop motif (residues 131-149), where the beta1 strand is flanked by strands beta2 and beta3. Moreover, a loop between strands beta3 and beta4 encompasses the helix beta3. Strands beta3-beta8 have antiparallel organization. The linker between the N- and C-terminal domains consists of residues between Val202 and Asp209. An extensive interface between the N- and C-terminal domains results in the rigidity of the entire structure, meaning that there is no hinge between the two domains, and they cannot move independently. The C-terminal domain, residues Leu210-Trp326, constitutes an alpha/beta/alpha fold, in which the mixed parallel/antiparallel beta-sheet is sandwiched between helices alpha6, eta7 (310 helix), and alpha8 from one side (close to the beta-sheet of the N-terminal domain) and eta4, alpha5, and alpha9 from the other. MtHPP dimeric assembly is stabilized by intermolecular Lys-CH2-Cys covalent bonds
additional information
-
covalent dimerization of MtHPP, a monomer of MtHPP has an alphabetaalphabetaalpha-sandwich-like arrangement. The N-terminal domain, which forms an alpha + beta structure, covers residues from the N-terminus to Glu201. Two long alpha-helices (alpha1 and alpha2) are separated by a mobile loop. The eight-stranded beta-sheet of the N-terminal domain contains a alpha-loop motif (residues 131-149), where the beta1 strand is flanked by strands beta2 and beta3. Moreover, a loop between strands beta3 and beta4 encompasses the helix beta3. Strands beta3-beta8 have antiparallel organization. The linker between the N- and C-terminal domains consists of residues between Val202 and Asp209. An extensive interface between the N- and C-terminal domains results in the rigidity of the entire structure, meaning that there is no hinge between the two domains, and they cannot move independently. The C-terminal domain, residues Leu210-Trp326, constitutes an alpha/beta/alpha fold, in which the mixed parallel/antiparallel beta-sheet is sandwiched between helices alpha6, eta7 (310 helix), and alpha8 from one side (close to the beta-sheet of the N-terminal domain) and eta4, alpha5, and alpha9 from the other. MtHPP dimeric assembly is stabilized by intermolecular Lys-CH2-Cys covalent bonds
additional information
the dimer is stabilized largely by hydrogen bonds, salt bridges, and van der Waals interactions. Asp189, Val149, Arg183, Asp202, Ala119, Arg171, Asn90, Arg93, Ile31, Arg122, and Ala186 of one monomer form hydrogen-bonding interactions with Arg185, Ile31, Asn90, Arg93, Arg122, Asp179, Tyr187, Gly199, Ser148, Gln121, and Ala186, respectively, of the other monomer and vice versa. There are two catalytic sites in the dimer, but only one product-exit channel shared by the two monomers at the dimer interface
additional information
-
the dimer is stabilized largely by hydrogen bonds, salt bridges, and van der Waals interactions. Asp189, Val149, Arg183, Asp202, Ala119, Arg171, Asn90, Arg93, Ile31, Arg122, and Ala186 of one monomer form hydrogen-bonding interactions with Arg185, Ile31, Asn90, Arg93, Arg122, Asp179, Tyr187, Gly199, Ser148, Gln121, and Ala186, respectively, of the other monomer and vice versa. There are two catalytic sites in the dimer, but only one product-exit channel shared by the two monomers at the dimer interface
additional information
-
the dimer is stabilized largely by hydrogen bonds, salt bridges, and van der Waals interactions. Asp189, Val149, Arg183, Asp202, Ala119, Arg171, Asn90, Arg93, Ile31, Arg122, and Ala186 of one monomer form hydrogen-bonding interactions with Arg185, Ile31, Asn90, Arg93, Arg122, Asp179, Tyr187, Gly199, Ser148, Gln121, and Ala186, respectively, of the other monomer and vice versa. There are two catalytic sites in the dimer, but only one product-exit channel shared by the two monomers at the dimer interface
-
additional information
-
the dimer is stabilized largely by hydrogen bonds, salt bridges, and van der Waals interactions. Asp189, Val149, Arg183, Asp202, Ala119, Arg171, Asn90, Arg93, Ile31, Arg122, and Ala186 of one monomer form hydrogen-bonding interactions with Arg185, Ile31, Asn90, Arg93, Arg122, Asp179, Tyr187, Gly199, Ser148, Gln121, and Ala186, respectively, of the other monomer and vice versa. There are two catalytic sites in the dimer, but only one product-exit channel shared by the two monomers at the dimer interface
-
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G195R
conserved Gly, required for histinol-phosphate phosphatase activity
D12A
-
shows only traces of the wild type activity
E18A
-
shows about 5% of the wild-type activity
D228N
the mutant shows reduced catalytic efficiency and kcat is reduced by approximately 6000fold compared to the wild type enzyme
E115Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
H42N
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R197M
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y117A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y117F
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Y157F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y161A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y161F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E115Q
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
R197M
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
Y117F
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
Y157F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
T151A
site-directed mutagenesis, inactive mutant
D213A
site-directed mutagenesis
D44A
site-directed mutagenesis
D83A
site-directed mutagenesis
E67A
site-directed mutagenesis
T88A
site-directed mutagenesis
D213A
-
site-directed mutagenesis
-
D44A
-
site-directed mutagenesis
-
D83A
-
site-directed mutagenesis
-
E67A
-
site-directed mutagenesis
-
T88A
-
site-directed mutagenesis
-
D213A
-
site-directed mutagenesis
-
D44A
-
site-directed mutagenesis
-
D83A
-
site-directed mutagenesis
-
E67A
-
site-directed mutagenesis
-
T88A
-
site-directed mutagenesis
-
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
additional information
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
additional information
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
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Staples, M.A.; Houston, L.L.
Purification of the bifunctional enzyme imidazoleglycerolphosphate dehydratase-histidinol phosphatase of Salmonella typhimurium
Biochim. Biophys. Acta
613
210-219
1980
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Brady, D.R.; Houston, L.L.
Some properties of the catalytic sites of imidazoleglycerol phosphate dehydratase-histidinol phosphate phosphatase, a bifunctional enzyme from Salmonella typhimurium
J. Biol. Chem.
248
2588-2592
1973
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Staples, M.A.; Houston, L.L.
Proteolytic degradation of imidazoleglycerolphosphate dehydratase-histidinol phosphatase from Salmonella typhimurium and the isolation of a resistant bifunctional core enzyme
J. Biol. Chem.
254
1395-1401
1979
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Sugiura, M.; Suzuki, S.; Kisumi M.
Improvement of histidine-producing strains of Serratia marcescens by cloning of a mutant allele of the histidine operon on a mini-F plasmid vector
Agric. Biol. Chem.
2
371-377
1987
Serratia marcescens
-
brenda
Carsiotis, M.; Jones R.F.
Cross-pathway regulation: tryptophan-mediated control of histidine and arginine biosynthetic enzymes in Neurospora crassa
J. Bacteriol.
119
889-892
1974
Neurospora crassa
brenda
Grisolia, V.; Carlomagno, M.S.; Bruni, C.B.
Cloning and expression of the distal portion of the histidine operon of Escherichia coli K-12
J. Bacteriol.
151
692-700
1982
Escherichia coli
brenda
Houston, L.L.; Graham, M.E.
Divalent metal Ion effects on a mutant histidinol phophate phosphatase from Samonella typhimurium
Arch. Biochem. Biophys.
162
513-522
1974
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium TA387
brenda
Araki, K.; Nakayama K.
A Biochemical characterization of histidine auxotrophs
Agric. Biol. Chem.
38
2219-2225
1974
Corynebacterium glutamicum
-
brenda
Houston, L.L.; Millay, Jr., H.
Effect of sulfhydryl reagents on the activity of histidinolphosphatase from Salmonella typhimurium and bakerss yeast
Biochim. Biophys. Acta
370
216-226
1974
Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Millay, H.; Houston, L.L.
Purification and properties of yeast histidinol phosphate phosphatase
Biochemistry
12
2591-2596
1973
Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Gorman j.A.; Hu, A.S.L.
The separation and partial characterization of L-histidinol phosphatase and an alkaline phosphatase of saccharomyces cerevisiae
J. Biol. Chem.
244
1645-1650
1969
Saccharomyces cerevisiae
brenda
Ames, B.N.
The biosynthesis of histidine: L-histidinol phosphate phosphatase
J. Biol. Chem.
226
583-593
1957
Escherichia coli, Neurospora crassa
brenda
Carsiotis, M.; Jones, R.F.; Wesseling, A.C.
Cross-pathway regulation: histidine-mediated control of histidine, tryptophan, and arginine biosynthetic enzymes in Neurospora crassa
J. Bacteriol.
119
893-898
1974
Neurospora crassa
brenda
Brady, D.R.; Houston, L.L.
New assay for histidinol phosphate phosphatase using a coupled reaction
Anal. Chem.
48
480-482
1972
Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Clark, M.A.; Baumann, L.; Baumann, P.
Buchnera aphidicola (aphid ndosymbiont) contains genes encoding enzymes of histidine biosynthesis
Curr. Microbiol.
37
356-358
1998
Buchnera aphidicola
brenda
le Coq, D.; Fillinger, S.; Aymerich, S.
Histidinol phosphate phosphatase, catalyzing the penultimate step of the histidine biosynthesis pathway, is encoded by ytvP (hisJ) in Bacillus subtilis
J. Bacteriol.
181
3277-3280
1999
Bacillus subtilis
brenda
Omi, R.; Goto, M.; Nakagawa, N.; Miyahara, I.; Hirotsu, K.
Expression, purification and preliminary X-ray characterization of histidinol phosphate phosphatase
Acta Crystallogr. Sect. D
60
574-576
2004
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Brilli, M.; Fani, R.
Molecular evolution of hisB genes
J. Mol. Evol.
58
225-237
2004
Salmonella enterica
brenda
Omi, R.; Goto, M.; Miyahara, I.; Manzoku, M.; Ebihara, A.; Hirotsu, K.
Crystal structure of monofunctional histidinol phosphate phosphatase from Thermus thermophilus HB8
Biochemistry
46
12618-12627
2007
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Marineo, S.; Cusimano, M.G.; Limauro, D.; Coticchio, G.; Puglia, A.M.
The histidinol phosphate phosphatase involved in histidine biosynthetic pathway is encoded by SCO5208 (hisN) in Streptomyces coelicolor A3(2)
Curr. Microbiol.
56
6-13
2008
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Lee, H.S.; Cho, Y.; Lee, J.H.; Kang, S.G.
Novel monofunctional histidinol-phosphate phosphatase of the DDDD superfamily of phosphohydrolases
J. Bacteriol.
190
2629-2632
2008
Thermococcus onnurineus
brenda
Rangarajan, E.S.; Proteau, A.; Wagner, J.; Hung, M.N.; Matte, A.; Cygler, M.
Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway
J. Biol. Chem.
281
37930-37941
2006
Escherichia coli
brenda
Jung, H.I.; Lee, H.S.; An, Y.J.; Cho, Y.; Lee, J.H.; Kang, S.G.; Cha, S.S.
Crystallization and preliminary X-ray crystallographic analysis of a novel histidinol-phosphate phosphatase from Thermococcus onnurineus NA1
Acta Crystallogr. Sect. F
65
472-474
2009
Thermococcus onnurineus NA1 (B1PRL6), Thermococcus onnurineus NA1
brenda
Petersen, L.N.; Marineo, S.; Mandala, S.; Davids, F.; Sewell, B.T.; Ingle, R.A.
The missing link in plant histidine biosynthesis: arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase
Plant Physiol.
152
1186-1196
2010
Arabidopsis thaliana (Q6NPM8)
brenda
Ghodge, S.V.; Fedorov, A.A.; Fedorov, E.V.; Hillerich, B.; Seidel, R.; Almo, S.C.; Raushel, F.M.
Structural and mechanistic characterization of L-histidinol phosphate phosphatase from the polymerase and histidinol phosphatase family of proteins
Biochemistry
52
1101-1112
2013
Lactococcus lactis subsp. lactis (Q02150), Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. lactis IL1403 (Q02150)
brenda
Kulis-Horn, R.K.; Persicke, M.; Kalinowski, J.
Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum
Microb. Biotechnol.
7
5-25
2014
Corynebacterium glutamicum (Q8NS80), Corynebacterium glutamicum
brenda
Kulis-Horn, R.; Rueckert, C.; Kalinowski, J.; Persicke, M.
Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond
BMC Microbiol.
17
161
2017
Corynebacterium glutamicum, Corynebacterium glutamicum (Q8NS79), Corynebacterium glutamicum (Q8NS80), Corynebacterium glutamicum LMG 3730 (Q8NS79), Corynebacterium glutamicum LMG 3730 (Q8NS80), Corynebacterium glutamicum ATCC 13032 (Q8NS79), Corynebacterium glutamicum ATCC 13032 (Q8NS80), Corynebacterium glutamicum JCM 1318 (Q8NS79), Corynebacterium glutamicum JCM 1318 (Q8NS80), Corynebacterium glutamicum NCIMB 10025 (Q8NS79), Corynebacterium glutamicum NCIMB 10025 (Q8NS80), Corynebacterium glutamicum DSM 20300, Corynebacterium glutamicum DSM 20300 (Q8NS79), Corynebacterium glutamicum DSM 20300 (Q8NS80)
brenda
Nourbakhsh, A.; Collakova, E.; Gillaspy, G.
Characterization of the inositol monophosphatase gene family in Arabidopsis
Front. Plant Sci.
5
725
2015
Arabidopsis thaliana (Q6NPM8)
brenda
Ruszkowski, M.; Dauter, Z.
Structural studies of Medicago truncatula histidinol phosphate phosphatase from inositol monophosphatase superfamily reveal details of penultimate step of histidine biosynthesis in plants
J. Biol. Chem.
291
9960-9973
2016
Medicago truncatula (G7J7Q5), Medicago truncatula
brenda
Jha, B.; Kumar, D.; Sharma, A.; Dwivedy, A.; Singh, R.; Biswal, B.K.
Identification and structural characterization of a histidinol phosphate phosphatase from Mycobacterium tuberculosis
J. Biol. Chem.
293
10102-10118
2018
Mycobacterium tuberculosis (P95189), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P95189), Mycobacterium tuberculosis ATCC 25618 (P95189)
brenda