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Information on EC 2.7.2.11 - glutamate 5-kinase and Organism(s) Bacillus subtilis and UniProt Accession Q6E235

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IUBMB Comments
In the absence of downstream enzymes, the product rapidly cyclizes to 5-oxo-L-proline and phosphate.
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This record set is specific for:
Bacillus subtilis
UNIPROT: Q6E235
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
gamma-glutamyl kinase, glutamate 5-kinase, glutamate kinase, gamma-gk, glutamate-5-kinase, gamma-glutamate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-glutamyl kinase
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ATP-L-glutamate 5-phosphotransferase
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ATP:gamma-L-glutamate phosphotransferase
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gamma-glutamate kinase
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gamma-glutamyl kinase
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gamma-glutamylphosphate kinase
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glutamate kinase
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GPK
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kinase (phosphorylating), glutamate
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kinase, glutamate (phosphorylating)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:L-glutamate 5-phosphotransferase
In the absence of downstream enzymes, the product rapidly cyclizes to 5-oxo-L-proline and phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
54596-30-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
show the reaction diagram
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-proline
completely inhibits the activity of wild-type gamma-glutamyl kinase/gamma-glutamyl phosphate reductase at concentrations greater than 0.1mM, and inhibits it by 30% at 0.01mM
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q6E235_BACIU
370
0
39671
TrEMBL
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N177D
mutant of the proBA fusion gene, improves the osmotolerance of host cells of Escherichia coli JM83, leads to overproduction of proline by host cells, is about 100fold less sensitive to proline-mediated feedback inhibition than the control
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
proBA fusion gene and mutated proBA fusion gene expressed in Escherichia coli JM83
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, M.; Cao, J.; Zheng, C.; Liu, Q.
Directed evolution of an artificial bifunctional enzyme, gamma-glutamyl kinase/gamma-glutamyl phosphate reductase, for improved osmotic tolerance of Escherichia coli transformants
FEMS Microbiol. Lett.
263
41-47
2006
Bacillus subtilis (Q6E235), Bacillus subtilis, Bacillus subtilis 93151-14 (Q6E235)
Manually annotated by BRENDA team