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Information on EC 3.1.1.31 - 6-phosphogluconolactonase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8LEV7

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.31 6-phosphogluconolactonase
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Arabidopsis thaliana
UNIPROT: Q8LEV7 not found.
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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
6-phosphogluconolactonase, 6pgl, phosphogluconolactonase, glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase, g6pd-6pgl, 6-pgl, 6-phosphogluconolactonase 3, 6-phosphoglucono-gamma-lactonase, xoo2316, og1rf_11582, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-phosphogluconolactonase
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6-PGL
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-
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6-phospho-D-glucose-delta-lactone hydrolase
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6-phosphoglucono-gamma-lactonase
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6-phosphogluconolactonase
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6-phosphogluconolactonase 3
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lactonase, phosphoglucono-
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PGL
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phosphogluconolactonase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-glucono-1,5-lactone lactonohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37278-45-8
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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
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co-localization with thioredoxin m-type, Trx_m2
Manually annotated by BRENDA team
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co-localization with thioredoxin m-type, Trx_m2
Manually annotated by BRENDA team
additional information
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PGL3 contains an N-terminal extension and a C-terminal peroxisome-targeting motif PTS1, subcellular localization of enzyme stages, overview. Besides redox-related and metabolic signals that influence dual-targeting of enzyme PGL3 in leaves, developmental and/or physiological state(s) play another role for subcellular enzyme localization in different plant parts, the metabolic state affects PGL3 targeting by absence/reduced stability of thioredoxin Trxm2
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
pgl3 mutation knocks out most of the 6PGL activity. Knockdown of PGL3 leads to a dramatic decrease in plant size, a significant increase in total glucose-6-phosphate dehydrogenase activity and a marked decrease in cellular redox potential. A wild-type PGL3-GFP transgene complements all phenotypes caused by the pgl3 mutation. Plastidic localization and enzymatic activity are required for PGL3 to complement the pgl3 mutant phenotypes. Pgl3 mutation exhibits constitutive pathogenesis-related gene expression and enhanced resistance to Pseudomonas syringae pv. maculicola ES4326 and Hyaloperonospora arabidopsidis Noco2. The pgl3 mutation activates NPR1- and SID2/EDS16/ICS1-dependent defense signaling
physiological function
PGL3 is the major contributor to total 6PGL activity. PGL3 is essential for plant growth and development. Plastidic localization and 6PGL activity of the PGL3 protein are essential for complementing all pgl3 phenotypes, indicating that the oxidative section of the plastidic pentose phosphate pathway is required for plant normal growth and development. PGL3 may function downstream of salicylic acid
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
6PGL5_ARATH
252
0
28476
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D150A
displays pgl3 morphology, does not complement the pgl3 phenotypes
D150A/D231A/H233A
displays pgl3 morphology, does not complement the pgl3 phenotypes
D231A/H233A
displays pgl3 morphology, does not complement the pgl3 phenotypes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
PCR product cloned into the corresponding sites of the vector pGEX-4T-1 and then introduced into Escherichia coli. Constructs (35S:DELTANTpgl3-GFP and 35S:pgl3 DELTASKL-GFP) together with the 35S:PGL3-GFP construct transformed into the pgl3 background. Escherichia coli cells expressing GST-PGL3 and GST-pgl3 mutants
gene PGL3, presence of the C-terminal SKL motif interfered with chloroplast import of a PGL3_N-full-CFP fusion and with that of a PGL3_long medial-CFP fusion (with free N- and C-terminal ends) exclusively labeling peroxisomes, co-expression of thioredoxin Trxm2 with C-terminally truncated enzyme PGL3_N-short and _N-long versions accumulate in the cytosol of tobacco protoplasts and co-localization with Trxm2 in the cytosol and in the chloroplast stroma, recombinant expression of N-terminally CFP-tagged, green-fluorescent enzyme in Nicotiana benthamiana leaves
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xiong, Y.; DeFraia, C.; Williams, D.; Zhang, X.; Mou, Z.
Characterization of Arabidopsis 6-phosphogluconolactonase T-DNA insertion mutants reveals an essential role for the oxidative section of the plastidic pentose phosphate pathway in plant growth and development
Plant Cell Physiol.
50
1277-1291
2009
Arabidopsis thaliana (Q84WW2), Arabidopsis thaliana (Q8LEV7), Arabidopsis thaliana (Q8LG70), Arabidopsis thaliana (Q9FIN1), Arabidopsis thaliana (Q9LMX8)
Manually annotated by BRENDA team
Hoelscher, C.; Meyer, T.; Von Schaewen, A.
Dual-targeting of Arabidopsis 6-phosphogluconolactonase 3 (PGL3) to chloroplasts and peroxisomes involves interaction with Trx m2 in the cytosol
Mol. Plant
7
252-255
2014
Arabidopsis thaliana
Manually annotated by BRENDA team