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Information on EC 2.7.1.71 - shikimate kinase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8GY88
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2.7.1.71 shikimate kinaseSpecify your search results
Word Map
- 2.7.1.71
- chorismate
-
shikimate-3-phosphate
- chrysanthemi
- oseltamivir
- dahp
-
5-enolpyruvylshikimate
-
3-deoxy-d-arabino-heptulosonate
- dehydroquinate
- 7-phosphate
- drug development
- synthesis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
shikimate kinase, shikimate kinase ii, atsk1, atsk2, ossk1, ossk2, sk ii, shikimate kinase-like 1, type ii shikimate kinase, ossk3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AroK
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-
-
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AroL
-
-
-
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kinase (phosphorylating), shikimate
-
-
-
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kinase, shikimate (phosphorylating)
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-
-
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shikimate kinase II
-
-
-
-
SKI
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-
-
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SKII
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-
SYSTEMATIC NAME
IUBMB Comments
ATP:shikimate 3-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9031-51-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
AtSK2 shikimate binding residues include Gly177, Gly178, Gly179, and Asp130 of the Walker B motif and Phe146, Phe154, Glu158, Arg155, and Arg243
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-
?
additional information
?
-
-
AtSK2 shikimate binding residues include Gly177, Gly178, Gly179, and Asp130 of the Walker B motif and Phe146, Phe154, Glu158, Arg155, and Arg243
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoform SK2 is predominantly expressed early in embryogenesis and vegetative tissues throughout development, isoform SK1 is expressed near or below background levels in vegetative tissues and is only expressed at higher levels in mature embryos and senescing leaves
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
AtSK2 belongs to the nucleoside monophosphate kinase family
metabolism
shikimate kinase catalyzes an intermediate step in the shikimate pathway to aromatic amino acid biosynthesis
malfunction
-
an enzyme-defective mutant exhibits an albino phenotype and has dramatically reduced chlorophyll content
metabolism
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shikimate kinase-like 1 does not function as shikimate kinase enzyme in the shikimate pathway but is involved in auxin-related pathways during chloroplast development
physiological function
-
the enzyme is essential for chloroplast development in Arabidopsis thaliana
additional information
additional information
mechanism of thermal regulation, computational analysis of AtSK1 and AtSK2 structural variation, overview
additional information
-
mechanism of thermal regulation, computational analysis of AtSK1 and AtSK2 structural variation, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SK2_ARATH
300
0
33777
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
AtSK2 adopts an alpha-beta-alpha fold with a central sheet of five parallel beta-strands flanked by two layers of alpha-helices. The AtSK2 structure can be divided into four domains: the reduced CORE domain comprising the central beta-sheet and flanking alpha-helices, the nucleotide binding domain, which includes the phosphate binding loop (P-loop/Walker-A motif), the disordered LID domain, which contains catalytic and substrate binding residues, and the extended shikimate binding domain, which includes a modified SK-type Walker B motif and several other substrate binding residues. Computational analysis of isozyme AtSK2 structure, overview
additional information
-
AtSK2 adopts an alpha-beta-alpha fold with a central sheet of five parallel beta-strands flanked by two layers of alpha-helices. The AtSK2 structure can be divided into four domains: the reduced CORE domain comprising the central beta-sheet and flanking alpha-helices, the nucleotide binding domain, which includes the phosphate binding loop (P-loop/Walker-A motif), the disordered LID domain, which contains catalytic and substrate binding residues, and the extended shikimate binding domain, which includes a modified SK-type Walker B motif and several other substrate binding residues. Computational analysis of isozyme AtSK2 structure, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heat-stable isozyme AtSK2, X-ray diffraction structure determinaion and analysis at 2.35 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K138N
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
K87R
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
L233F
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
N234K
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
R120K
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
S152N
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
S251N
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
T230S
AtSK1 mutation relative to AtSK2 predicted to confer substantial stabilizing effect
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
isozyme AtSK2 is highly unstable and becomes inactivated at 37°C, whereas the heat-induced isoform, AtSK1, is thermostable and fully active at 37°C
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene expression patterns of isoforms, AtSK1 and AtSK2 showing a signature of regulatory subfunctionalization
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of plant shikimate kinase is induced under specific conditions of environmental stress and developmental requirements in an isoform-specific manner
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fucile, G.; Falconer, S.; Christendat, D.
Evolutionary diversification of plant shikimate kinase gene duplicates
PLoS Genet.
4
e1000292
2008
Arabidopsis thaliana
Fucile, G.; Garcia, C.; Carlsson, J.; Sunnerhagen, M.; Christendat, D.
Structural and biochemical investigation of two Arabidopsis shikimate kinases: the heat-inducible isoform is thermostable
Protein Sci.
20
1125-1136
2011
Arabidopsis thaliana (Q8GY88), Arabidopsis thaliana
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