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Information on EC 5.3.1.9 - glucose-6-phosphate isomerase and Organism(s) Arabidopsis thaliana

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IUBMB Comments
The enzyme from yeast catalyses the reversible conversion specifically between the alpha-D-glucose 6-phosphate and beta-D-fructofuranose 6-phosphate. The enzyme also catalyses the anomerization of both D-hexose 6-phosphates .
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This record set is specific for:
Arabidopsis thaliana
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphoglucose isomerase, glucose-6-phosphate isomerase, glucose phosphate isomerase, autocrine motility factor, phosphoglucoisomerase, phosphohexose isomerase, neuroleukin, pgi/amf, amf/pgi, glucose 6-phosphate isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-Phosphoglucose isomerase
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D-Glucose-6-phosphate isomerase
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D-glucose-6-phosphate ketol-isomerase
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Glucose 6-phosphate isomerase
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Glucose phosphate isomerase
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Glucose phosphoisomerase
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glucose-6-phosphate isomerase, cytosolic
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Glucosephosphate isomerase 2
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GPI
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Hexose 6-phosphate isomerase
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Hexose isomerase
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Hexose monophosphate isomerase
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Hexose phosphate isomerase
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Hexosephosphate isomerase
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Isomerase, glucose phosphate
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Neuroleukin
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NLK
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-
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Oxoisomerase
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PGI
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-
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PGI2
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PGI3
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PHI
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Phosphoglucoisomerase
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Phosphoglucose isomerase
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Phosphohexoisomerase
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Phosphohexomutase
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Phosphohexose isomerase
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Phosphosaccharomutase
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SA-36
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Sperm antigen-36
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VEG54
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Vegetative protein 54
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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isomerization
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose-6-phosphate aldose-ketose-isomerase (configuration-inverting)
The enzyme from yeast catalyses the reversible conversion specifically between the alpha-D-glucose 6-phosphate and beta-D-fructofuranose 6-phosphate. The enzyme also catalyses the anomerization of both D-hexose 6-phosphates [7].
CAS REGISTRY NUMBER
COMMENTARY hide
9001-41-6
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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
starch content in leaves completely lacking PGI1 activity is about 10-15% of that of wild type leaves and can be be reverted by the introduction of a sex1 null mutation impeding beta-amylolytic starch breakdown. In mutant strains, starch granules are present in the chloroplasts of mesophyll cells and plastidic and extra-plastidic beta-amylase encoding genes are higly expressed in leaves. Mutant strains display slow growth and reduced photosynthetic capacity phenotypes even under continuous light conditions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G6PI_ARATH
560
0
61718
Swiss-Prot
other Location (Reliability: 1)
G6PIP_ARATH
613
0
67048
Swiss-Prot
Chloroplast (Reliability: 1)
Q84J52_ARATH
116
0
12785
TrEMBL
other Location (Reliability: 3)
A0A178UPP5_ARATH
560
0
61718
TrEMBL
other Location (Reliability: 1)
A0A178UUU3_ARATH
613
0
67048
TrEMBL
Chloroplast (Reliability: 1)
A0A1P8BG38_ARATH
528
0
58109
TrEMBL
other Location (Reliability: 3)
A0A7G2F587_ARATH
646
0
70979
TrEMBL
Chloroplast (Reliability: 1)
A0A090MHY5_ARATH
611
0
66807
TrEMBL
Chloroplast (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Agrobacterium tumefaciens
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (P34795)
Manually annotated by BRENDA team
Bahaji, A.; Sanchez-Lopez, A.M.; De Diego, N.; Munoz, F.J.; Baroja-Fernandez, E.; Li, J.; Ricarte-Bermejo, A.; Baslam, M.; Aranjuelo, I.; Almagro, G.; Humplik, J.F.; Novak, O.; Spichal, L.; Dolezal, K.; Pozueta-Romero, J.
Plastidic phosphoglucose isomerase is an important determinant of starch accumulation in mesophyll cells, growth, photosynthetic capacity, and biosynthesis of plastidic cytokinins in Arabidopsis
PLoS ONE
10
e0119641
2015
Arabidopsis thaliana (A0A090MHY5)
Manually annotated by BRENDA team