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Information on EC 1.2.1.70 - glutamyl-tRNA reductase and Organism(s) Arabidopsis thaliana and UniProt Accession P42804

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IUBMB Comments
This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway. The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the alpha-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37.
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Arabidopsis thaliana
UNIPROT: P42804
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glutamyl-trna reductase, glutr, hema1, hema2, glutr1, athema1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutamyl-tRNA reductase
-
-
GluTR1
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isoform
SYSTEMATIC NAME
IUBMB Comments
L-glutamate-semialdehyde:NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming)
This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway. The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the alpha-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37.
CAS REGISTRY NUMBER
COMMENTARY hide
119940-26-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
show the reaction diagram
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-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
show the reaction diagram
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
-
-
-
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
protein FLU
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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
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2,4-diphenyl-6-styryl-1-p-tolyl-pyridinium boron tetrafluoride
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IC50: 0.01 mM
4-[4-(3,4-dihydroxyphenyl)-2,3-dimethylbutyl]benzene-1,2-diol
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IC50: 0.055 mM
5,6-dichloro-1,3-benzodioxol-2-one
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IC50: 0.055 mM
fluorescent in blue light
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FLU, the protein mediates inactivation of the enzyme at the membrane
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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)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GluBP regulator
the GluTR regulator, GluTR binding protein (GluBP), spatially organizes tetrapyrrole synthesis by distributing enzyme GluTR into different suborganellar locations. GluBP belongs to a heme-binding family involved in heme metabolism. Complex structure of GluTR-GluBP from Arabidopsis thaliana, overview. The dimeric GluBP binds symmetrically to the catalytic domains of the V-shaped GluTR dimer via its C-terminal domain. A substantial conformational change of the GluTR NADPH-binding domain is observed, confirming the postulated rotation of the NADPH-binding domain for hydride transfer from NADPH to the substrate. Arg146, guarding the door for metabolic channeling, adopts alternative conformations, which may represent steps involved in substrate recognition and product release. GluBP stimulates GluTR catalytic efficiency with an approximate 3fold increase of the 5-aminolevulinic acid formation rate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde. GluBP stimulates GluTR activity and regulates GSA release
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cycloheximide
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Ozone
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induces expression in photosynthetic tissues
additional information
-
is induced in photosynthetic tissues by oxidative stresses such as wounding
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
2,4-diphenyl-6-styryl-1-p-tolyl-pyridinium boron tetrafluoride
Arabidopsis thaliana
-
IC50: 0.01 mM
0.055
4-[4-(3,4-dihydroxyphenyl)-2,3-dimethylbutyl]benzene-1,2-diol
Arabidopsis thaliana
-
IC50: 0.055 mM
0.055
5,6-dichloro-1,3-benzodioxol-2-one
Arabidopsis thaliana
-
IC50: 0.055 mM
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
spatial organization of 5-aminolevulinic acid formation in chloroplasts. The majority of a glutamyl-tRNA reductase (GluTR) and glutamate-1 semialdehyde aminotransferase (GSAT) protein complex is located in the stroma and forms delta-aminolevulinic acid (ALA) starting with glutamyltRNAGlu, while a minor part of the active protein complex is attached to the thylakoid membrane via a GluTR-binding protein (GluTRBP)
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
physiological function
metabolism
physiological function
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the enzyme is required for the biosynthesis of 5-aminolevulinic acid. Formation of 5-aminolevulinic acid at the beginning of the pathway is the rate limiting step of tetrapyrrole biosynthesis and target of multiple timely and spatially organized control mechanisms. Regulation of the pathway, detailed overview. Spatial organization of 5-aminolevulinic acid formation in chloroplasts. The majority of a glutamyl-tRNA reductase (GluTR) and glutamate-1 semialdehyde aminotransferase (GSAT) protein complex is located in the stroma and forms 5-aminolevulinic acid starting with glutamyltRNAGlu, while a minor part of the active protein complex is attached to the thylakoid membrane via a GluTR-binding protein (GluTRBP). At night the FLU protein, another glutamyl-tRNA reductase binding protein, binds the soluble glutamyl-tRNA reductase fraction to the thylakoid membrane and thereby inactivates 5-aminolevulinic acid formation. Only the GluTRBP bound fraction of GluTR can continue to synthesize 5-aminolevulinic acid during dark periods, preventing both a lack of heme during darkness and excessive accumulation of phototoxic intermediates of chlorophyll biosynthesis. The FLU protein i a negative regulator of 5-aminolevulinic acid biosynthesis
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)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HEM11_ARATH
543
0
59515
Swiss-Prot
Chloroplast (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GluTR consists of three domains: an N-terminal catalytic domain, an NADPH-binding domain, and a C-terminal dimerization domain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified GluTR in complex with GluBP, X-ray diffraction structure determination and analysis at 2.8 A resolution, modeling
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
uncomplexed TPR domain of FLU (FLUTPR) and complex of the dimeric domain of GluTR bound to FLUTPR, hanging drop vapor diffusion method, from 0.2 M NaCl, 0.1 M Bis-Tris, pH 6.5, and 25% w/v PEG 3350 in 1 week, and from 0.15 M KBr and 30% w/v PEG monomethyl ether 2000, in 3 weeks, X-ray diffraction structure determination and analysis at 1.45 and 2.4 A resolution, respectively, molecular replacement and modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the binding of the protein fluorescent in blue light enhances the enzyme stability
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the chaperone for light-harvesting chlorophyll a/b-binding proteins, the chloroplast SRP43, directly binds to and prevents aggregation of the enzyme, thereby enhancing the stability of active enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged FLUTPR and GluTRDD in Escherichia coli strain BL21(DE3)
Ni-NTA column chromatography and glutathione Sepharose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene HEMA1, recombinant co-overexpression of N-terminally His6-tagged FLUTPR and GluTRDD in Escherichia coli strain BL21(DE3)
AtHemA1 overexpression in Nicotiana tabacum cv Samsun NN using Agrobacterium tumefaciens and Arabidopsis thaliana by transformation
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expressed in Escherichia coli BL21 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of HEMA1 that encodes the dominant GluTR in the photosynthetic tissues is regulated by light
a rapidly decreased content of soluble enzyme is observed in wild type seedlings within the first 3 h in darkness
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expression profiles in the first hours of deetiolation of Arabidopsis seedlings show an abundance of GluTR that gradually increased with chlorophyll biosynthesis
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stromal enzyme content reaches a maximum at day 14 during short days (10 h light/14 h darkness) and continuous light conditions, before it visibly decreases at day 40. Maximum membrane-bound enzyme is found at day 28 during short days and at days 14 and 28 under continuous light
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the tetrapyrrole biosynthetic pathway is controlled by HEMA2 and FC1, which normally functions for heme biosynthesis in nonphotosynthetic tissues, but is induced in photosynthetic tissues under oxidative conditions to supply heme for defensive hemoproteins outside plastids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loida, P.J.; Thompson, R.L.; Walker, D.M.; CaJacob, C.A.
Novel inhibitors of glutamyl-tRNA(Glu) reductase identified through cell-based screening of the heme/chlorophyll biosynthetic pathway
Arch. Biochem. Biophys.
372
230-237
1999
Arabidopsis thaliana
Manually annotated by BRENDA team
Nagai, S.; Koide, M.; Takahashi, S.; Kikuta, A.; Aono, M.; Sasaki-Sekimoto, Y.; Ohta, H.; Takamiya, K.; Masuda, T.
Induction of isoforms of tetrapyrrole biosynthetic enzymes, AtHEMA2 and AtFC1, under stress conditions and their physiological functions in Arabidopsis
Plant Physiol.
144
1039-1051
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Schmied, J.; Hedtke, B.; Grimm, B.
Overexpression of HEMA1 encoding glutamyl-tRNA reductase
J. Plant Physiol.
168
1372-1379
2011
Arabidopsis thaliana
Manually annotated by BRENDA team
Czarnecki, O.; Hedtke, B.; Melzer, M.; Rothbart, M.; Richter, A.; Schroeter, Y.; Pfannschmidt, T.; Grimm, B.
An Arabidopsis GluTR binding protein mediates spatial separation of 5-aminolevulinic acid synthesis in chloroplasts
Plant Cell
23
4476-4491
2011
Arabidopsis thaliana
Manually annotated by BRENDA team
Zhang, M.; Zhang, F.; Fang, Y.; Chen, X.; Chen, Y.; Zhang, W.; Dai, H.E.; Lin, R.; Liu, L.
The non-canonical tetratricopeptide repeat (TPR) domain of fluorescent (FLU) mediates complex formation with glutamyl-tRNA reductase
J. Biol. Chem.
290
17559-17565
2015
Arabidopsis thaliana (P42804)
Manually annotated by BRENDA team
Czarnecki, O.; Grimm, B.
New insights in the topology of the biosynthesis of 5-aminolevulinic acid
Plant Signal. Behav.
8
e23124
2013
Arabidopsis thaliana
Manually annotated by BRENDA team
Zhao, A.; Fang, Y.; Chen, X.; Zhao, S.; Dong, W.; Lin, Y.; Gong, W.; Liu, L.
Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein
Proc. Natl. Acad. Sci. USA
111
6630-6635
2014
Arabidopsis thaliana (P42804), Arabidopsis thaliana
Manually annotated by BRENDA team
Fang, Y.; Zhao, S.; Zhang, F.; Zhao, A.; Zhang, W.; Zhang, M.; Liu, L.
The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein
Sci. Rep.
6
19756
2016
Arabidopsis thaliana (P42804)
Manually annotated by BRENDA team
Richter, A.S.; Banse, C.; Grimm, B.
The GluTR-binding protein is the heme-binding factor for feedback control of glutamyl-tRNA reductase
eLife
8
e46300
2019
Arabidopsis thaliana
Manually annotated by BRENDA team
Schmied, J.; Hou, Z.; Hedtke, B.; Grimm, B.
Controlled partitioning of glutamyl-tRNA reductase in stroma- and membrane-associated fractions affects the synthesis of 5-aminolevulinic acid
Plant Cell Physiol.
59
2204-2213
2018
Arabidopsis thaliana
Manually annotated by BRENDA team
Hou, Z.; Yang, Y.; Hedtke, B.; Grimm, B.
Fluorescence in blue light (FLU) is involved in inactivation and localization of glutamyl-tRNA reductase during light exposure
Plant J.
97
517-529
2019
Arabidopsis thaliana
Manually annotated by BRENDA team
Wang, P.; Liang, F.C.; Wittmann, D.; Siegel, A.; Shan, S.O.; Grimm, B.
Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis
Proc. Natl. Acad. Sci. USA
115
E3588-E3596
2018
Arabidopsis thaliana
Manually annotated by BRENDA team