BRENDA - Enzyme Database

The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein

Fang, Y.; Zhao, S.; Zhang, F.; Zhao, A.; Zhang, W.; Zhang, M.; Liu, L.; Sci. Rep. 6, 19756 (2016)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.2.1.70
gene HEMA1
Arabidopsis thaliana
Crystallization (Commentary)
EC Number
Crystallization
Organism
1.2.1.70
purified recombinant GluTR in ternary complex with GBP and FLUTPR, the protein are mixed at molar ratio of 2:3:3, X-ray diffraction structure determination and analysis at 3.2 A resolution, molecular replacement method
Arabidopsis thaliana
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.1.70
heme
feedback inhibition
Arabidopsis thaliana
1.2.1.70
additional information
structure analysis of the FLUTPR-GluTR-GBP ternary complex, overview. Three mechanisms for plant GluTR activity regulation: (i) the end-product feedback inhibition by heme, (ii) repression by a membrane protein FLUORESCENT (FLU), and (iii) formation of complex with a soluble GluTR-binding protein (GBP)
Arabidopsis thaliana
1.2.1.70
protein FLU
membrane protein FLUORESCENT, protein FLU directly interacts with GluTR's dimerization domain through its tetratricopepetide-repeat (TPR) domain. Enzyme binding structure, overview
Arabidopsis thaliana
1.2.1.70
protein GBP
a soluble GluTR-binding protein, enzyme binding structure, overview. the GluTR-GBP complex is stable and has a low apparent dissociation constant. Protein GBP is initially found in chloroplast stroma
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
Arabidopsis thaliana
-
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.70
Arabidopsis thaliana
P42804
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
743807
Arabidopsis thaliana
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.2.1.70
More
GluTR consists of three domains: an N-terminal catalytic domain, an NADPH-binding domain, and a C-terminal dimerization domain
Arabidopsis thaliana
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.70
NADP+
-
Arabidopsis thaliana
1.2.1.70
NADPH
-
Arabidopsis thaliana
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.1.70
gene HEMA1
Arabidopsis thaliana
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.70
NADP+
-
Arabidopsis thaliana
1.2.1.70
NADPH
-
Arabidopsis thaliana
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.2.1.70
purified recombinant GluTR in ternary complex with GBP and FLUTPR, the protein are mixed at molar ratio of 2:3:3, X-ray diffraction structure determination and analysis at 3.2 A resolution, molecular replacement method
Arabidopsis thaliana
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.1.70
heme
feedback inhibition
Arabidopsis thaliana
1.2.1.70
additional information
structure analysis of the FLUTPR-GluTR-GBP ternary complex, overview. Three mechanisms for plant GluTR activity regulation: (i) the end-product feedback inhibition by heme, (ii) repression by a membrane protein FLUORESCENT (FLU), and (iii) formation of complex with a soluble GluTR-binding protein (GBP)
Arabidopsis thaliana
1.2.1.70
protein FLU
membrane protein FLUORESCENT, protein FLU directly interacts with GluTR's dimerization domain through its tetratricopepetide-repeat (TPR) domain. Enzyme binding structure, overview
Arabidopsis thaliana
1.2.1.70
protein GBP
a soluble GluTR-binding protein, enzyme binding structure, overview. the GluTR-GBP complex is stable and has a low apparent dissociation constant. Protein GBP is initially found in chloroplast stroma
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
Arabidopsis thaliana
-
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
743807
Arabidopsis thaliana
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.2.1.70
More
GluTR consists of three domains: an N-terminal catalytic domain, an NADPH-binding domain, and a C-terminal dimerization domain
Arabidopsis thaliana
Expression
EC Number
Organism
Commentary
Expression
1.2.1.70
Arabidopsis thaliana
expression of HEMA1 that encodes the dominant GluTR in the photosynthetic tissues is regulated by light
up
General Information
EC Number
General Information
Commentary
Organism
1.2.1.70
metabolism
plants synthesize delta-aminolevulenic acid (ALA), the precursor for all tetrapyrrole molecules, from glutamate via a three-step pathway1 The first step is ligation of glutamate to tRNAGlu catalyzed by glutamyl-tRNA synthetase. Then glutamyl-tRNA reductase (GluTR) reduces the tRNAGlu-bound glutamate to glutamate-1-semialdehyde (GSA) in an NADPH-dependent manner. GSA is subsequently isomerized to ALA by a vitamin B6-dependent enzyme, glutamate-1-semialdehyde aminomutase (GSAM). 5-Aminolevulinic acid synthesis is the key regulatory point for the entire tetrapyrrole biosynthetic pathway, and particularly GluTR is subjected to a tight control at the post-translational level
Arabidopsis thaliana
1.2.1.70
additional information
three mechanisms for plant GluTR activity regulation: (i) the end-product feedback inhibition by heme, (ii) repression by a membrane protein FLUORESCENT (FLU), and (iii) formation of complex with a soluble GluTR-binding protein (GBP)
Arabidopsis thaliana
1.2.1.70
physiological function
the GluTR-catalyzed glutamyl-tRNAGlu reduction by NADPH is a key regulatory point of the tetrapyrrole biosynthetic pathway. Plants synthesize delta-aminolevulenic acid (ALA), the precursor for all tetrapyrrole molecules, from glutamate via a three-step pathway. The first step is ligation of glutamate to tRNAGlu catalyzed by glutamyl-tRNA synthetase. Then glutamyl-tRNA reductase (GluTR) reduces the tRNAGlu-bound glutamate to glutamate-1-semialdehyde (GSA) in an NADPH-dependent manner. GSA is subsequently isomerized to 5-aminolevulinic acid by a vitamin B6-dependent enzyme, glutamate-1-semialdehyde aminomutase (GSAM). 5-Aminolevulinic acid synthesis is the key regulatory point for the entire tetrapyrrole biosynthetic pathway, and particularly GluTR is subjected to a tight control at the post-translational level. Regulation of the enzyme within the pathway, detailed overview. Glutamate-1-semialdehyde aminomutase (GSAM) is proposed to form complex with GluTR to enable GSA channeling from GluTR to GSAM in bacteria, but not in plants
Arabidopsis thaliana
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.2.1.70
metabolism
plants synthesize delta-aminolevulenic acid (ALA), the precursor for all tetrapyrrole molecules, from glutamate via a three-step pathway1 The first step is ligation of glutamate to tRNAGlu catalyzed by glutamyl-tRNA synthetase. Then glutamyl-tRNA reductase (GluTR) reduces the tRNAGlu-bound glutamate to glutamate-1-semialdehyde (GSA) in an NADPH-dependent manner. GSA is subsequently isomerized to ALA by a vitamin B6-dependent enzyme, glutamate-1-semialdehyde aminomutase (GSAM). 5-Aminolevulinic acid synthesis is the key regulatory point for the entire tetrapyrrole biosynthetic pathway, and particularly GluTR is subjected to a tight control at the post-translational level
Arabidopsis thaliana
1.2.1.70
additional information
three mechanisms for plant GluTR activity regulation: (i) the end-product feedback inhibition by heme, (ii) repression by a membrane protein FLUORESCENT (FLU), and (iii) formation of complex with a soluble GluTR-binding protein (GBP)
Arabidopsis thaliana
1.2.1.70
physiological function
the GluTR-catalyzed glutamyl-tRNAGlu reduction by NADPH is a key regulatory point of the tetrapyrrole biosynthetic pathway. Plants synthesize delta-aminolevulenic acid (ALA), the precursor for all tetrapyrrole molecules, from glutamate via a three-step pathway. The first step is ligation of glutamate to tRNAGlu catalyzed by glutamyl-tRNA synthetase. Then glutamyl-tRNA reductase (GluTR) reduces the tRNAGlu-bound glutamate to glutamate-1-semialdehyde (GSA) in an NADPH-dependent manner. GSA is subsequently isomerized to 5-aminolevulinic acid by a vitamin B6-dependent enzyme, glutamate-1-semialdehyde aminomutase (GSAM). 5-Aminolevulinic acid synthesis is the key regulatory point for the entire tetrapyrrole biosynthetic pathway, and particularly GluTR is subjected to a tight control at the post-translational level. Regulation of the enzyme within the pathway, detailed overview. Glutamate-1-semialdehyde aminomutase (GSAM) is proposed to form complex with GluTR to enable GSA channeling from GluTR to GSAM in bacteria, but not in plants
Arabidopsis thaliana
Expression (protein specific)
EC Number
Organism
Commentary
Expression
1.2.1.70
Arabidopsis thaliana
expression of HEMA1 that encodes the dominant GluTR in the photosynthetic tissues is regulated by light
up