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Information on EC 2.5.1.30 - heptaprenyl diphosphate synthase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P55784

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IUBMB Comments
This enzyme catalyses the condensation reactions resulting in the formation of all-trans-heptaprenyl diphosphate, the isoprenoid side chain of ubiquinone-7 and menaquinone-7. The enzyme adds four isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
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This record set is specific for:
Geobacillus stearothermophilus
UNIPROT: P55784 not found.
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The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
heptaprenyl diphosphate synthase, hepps, heptaprenyl pyrophosphate synthetase, heppps, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 4 isopentenyl units)
This enzyme catalyses the condensation reactions resulting in the formation of all-trans-heptaprenyl diphosphate, the isoprenoid side chain of ubiquinone-7 and menaquinone-7. The enzyme adds four isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
CAS REGISTRY NUMBER
COMMENTARY hide
74506-59-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P55784: subunit 1, P55785: subunit 2
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HEPS1_GEOSE
220
0
24636
Swiss-Prot
-
HEPS2_GEOSE
320
0
35808
Swiss-Prot
-
A0A150NDS0_GEOSE
263
0
29542
TrEMBL
-
A0A150NDV8_GEOSE
320
0
35812
TrEMBL
-
A0A087LFB8_GEOSE
320
0
35808
TrEMBL
-
A0A150MKF3_GEOSE
263
0
29610
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24610
x * 24610 (subunit 1) + x * 36172 (subunit 2), calculated from sequence
36172
x * 24610 (subunit 1) + x * 36172 (subunit 2), calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 24610 (subunit 1) + x * 36172 (subunit 2), calculated from sequence
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koike-Takeshita, A.; Koyama, T.; Ogura, K.
Intersubunit structure within heterodimers of medium-chain prenyl diphosphate synthases. Formation of a hybrid-type heptaprenyl diphosphate synthase
J. Biochem.
124
790-797
1998
Geobacillus stearothermophilus (P55784 and P55785), Geobacillus stearothermophilus
Manually annotated by BRENDA team
Koike-Takeshita, A.; Koyama, T.; Obata, S.; Ogura, K.
Molecular cloning and nucleotide sequences of the genes for two essential proteins constituting a novel enzyme system for heptaprenyl diphosphate synthesis
J. Biol. Chem.
270
18396-18400
1995
Geobacillus stearothermophilus (P55784 and P55785), Geobacillus stearothermophilus
Manually annotated by BRENDA team