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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.6.5 - GTP diphosphokinase and Organism(s) Streptomyces antibioticus and UniProt Accession Q53597

for references in articles please use BRENDA:EC2.7.6.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.6 Diphosphotransferases
                2.7.6.5 GTP diphosphokinase
IUBMB Comments
GDP can also act as acceptor.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Streptomyces antibioticus
UNIPROT: Q53597
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: Streptomyces antibioticus
The enzyme appears in selected viruses and cellular organisms
Synonyms
(p)ppgpp synthetase, stringent factor, relmtb, (p)ppgpp synthase, alarmone synthetase, gtp pyrophosphokinase, sas 1, (p)ppgpp synthetase i, guanosine pentaphosphate synthetase, atp:gtp 3'-pyrophosphotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(p)ppGpp synthetase I
-
-
-
-
(p)ppGpp synthetase II
-
-
-
-
ATP-GTP 3'-diphosphotransferase
-
-
-
-
GPSI
-
-
-
-
GPSII
-
-
-
-
GTP pyrophosphokinase
-
-
-
-
guanosine 3',5'-polyphosphate synthase
-
-
-
-
guanosine 3',5'-polyphosphate synthetase
-
-
-
-
guanosine 5',3'-polyphosphate synthetase
-
-
-
-
guanosine pentaphosphate synthetase
-
-
-
-
stringent factor
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
show the reaction diagram
bifunctional enzyme, additionally has polynucleotide phosphorylase activities
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphosphate transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:GTP 3'-diphosphotransferase
GDP can also act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
63690-89-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
show the reaction diagram
-
-
-
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
show the reaction diagram
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dCDP
slightly stimulates synthesis of guanosine 3'-diphosphate 5'-triphosphate, inhibits polynucleotide phosphorylase activities of enzyme
methanol
-
maximal stimulation of GPSI by 20% v/v
mRNA
-
synthetic, e.g. poly(U), stimulates, level of stimulation is greater in presence of RNA and poly(U) together than with either RNA alone, no activation by ribosomes
tRNA
-
uncharged or charged, stimulation, level of stimulation is greater in presence of RNA and poly(U) together than with either RNA alone
Trypsin
-
incubation with low levels of trypsin activates
-
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PNP_STRAT
740
0
79160
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
-
1 * 47000, GPS II, produced by proteolysis of the larger 88000 MW form, denaturing PAGE, 1 * 88000, GPS I, denaturing PAGE
88000
-
1 * 47000, GPS II, produced by proteolysis of the larger 88000 MW form, denaturing PAGE, 1 * 88000, GPS I, denaturing PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 47000, GPS II, produced by proteolysis of the larger 88000 MW form, denaturing PAGE, 1 * 88000, GPS I, denaturing PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jones, G.H.
Purification and properties of ATP:GTP 3-pyrophosphotransferase (guanosine pentaphosphate synthetase) from Streptomyces antibioticus
J. Bacteriol.
176
1475-1481
1994
Saccharopolyspora erythraea, Streptomyces albus, Streptomyces ambofaciens, Streptomyces antibioticus, Streptomyces anulatus, Streptomyces coelicolor, Streptomyces fradiae, Streptomyces fradiae UC8306, Streptomyces glaucescens, Streptomyces glaucescens ETH 22794, Streptomyces lividans, Streptomyces lividans TK24, Streptomyces parvulus
Manually annotated by BRENDA team
Jones, G.H.
Activation of ATP:GTP 3-pyrophosphotransferase (guanosine pentaphosphate synthetase) in Streptomyces antibioticus
J. Bacteriol.
176
1482-1487
1994
Streptomyces antibioticus
Manually annotated by BRENDA team
Jones, G.H.; Bibb, M.J.
Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase
J. Bacteriol.
178
4281-4288
1996
Streptomyces antibioticus (Q53597), Streptomyces antibioticus
Manually annotated by BRENDA team