Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.4.21 - inositol-hexakisphosphate 5-kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q12494

for references in articles please use BRENDA:EC2.7.4.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Three mammalian isoforms are known to exist.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q12494
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
ip6k1, ip6k2, ip6k3, ppip5k1, ppip5k2, insp6k2, inositol hexakisphosphate kinase, inositol hexakisphosphate kinase 1, ihpk2, atvip1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP:1D-myo-inositol-hexakisphosphate phosphotransferase
-
-
-
-
diphosphoinositol pentakisphosphate synthetase
-
-
-
-
inositol hexakisphosphate kinase
-
-
-
-
InsP6 kinase
-
-
-
-
InsP6K3
-
-
-
-
IP6 kinase
-
-
-
-
IP6K
-
-
-
-
kinase (phosphorylating), inositol hexakisphosphate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho-group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol-hexakisphosphate 5-phosphotransferase
Three mammalian isoforms are known to exist.
CAS REGISTRY NUMBER
COMMENTARY hide
176898-37-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene KCS1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
deletion of KCS1, which blocks synthesis of inositol diphosphates on the 5-hydroxyl of the inositol ring, causes inositol auxotrophy and decreased intracellular inositol and phosphatidylinositol levels. These defects are caused by a profound decrease in transcription of INO1, which encodes myo-inositol-3-phosphate synthase. Expression of genes that function in glycolysis, transcription, and protein processing is not affected in kcs1DELTA. Deletion of OPI1, the INO1 transcription repressor, does not fully rescue INO1 expression in kcs1DELTA. Decreased inositol biosynthesis in kcs1DELTA is due to downregulation of INO1 transcription, but decreased inositol biosynthesis in kcs1DELTA is not because of perturbation of the UASINO regulatory complex Opi1-Ino2-Ino4, overview
physiological function
modulation of Kcs1 controls INO1 transcription by regulating synthesis of inositol diphosphates, model of regulation of INO1 transcription by Kcs1 and inositol diphosphates, overview. bZIP and inositol pyrophosphate kinase (DINS) domains of enzyme Kcs1 are required for INO1 transcription. The Kcs1 protein, but not transcription, is regulated in response to inositol
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ye, C.; Bandara, W.M.; Greenberg, M.L.
Regulation of inositol metabolism is fine-tuned by inositol pyrophosphates in Saccharomyces cerevisiae
J. Biol. Chem.
288
24898-24908
2013
Saccharomyces cerevisiae (Q12494)
Manually annotated by BRENDA team