Information on EC 3.6.3.48 - alpha-factor-transporting ATPase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.3.48
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RECOMMENDED NAME
GeneOntology No.
alpha-factor-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + alpha-factor/in = ADP + phosphate + alpha-factor/out
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphate bond
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transmembrane transport
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (alpha-factor-transporting)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports the alpha-factor sex pheromone.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
gene STE6
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Manually annotated by BRENDA team
strain RKY959 MATa his3-DELTA200 leu2-3,112 lys2-801 DELTAste6::LEU2 trp1-DELTA63 ura3-52
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + alpha-factor/in
ADP + phosphate + alpha-factor/out
show the reaction diagram
ATP + H2O + alpha-factor/in
ATP + H2O + alpha-factor/in
show the reaction diagram
additional information
?
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Ste6p plays an essential role in the export of farnesyl-modified a-type mating factors, close relationship between the ability of this class of transporters to export drugs and lipid-modified signaling molecules
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + alpha-factor/in
ADP + phosphate + alpha-factor/out
show the reaction diagram
additional information
?
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Ste6p plays an essential role in the export of farnesyl-modified a-type mating factors, close relationship between the ability of this class of transporters to export drugs and lipid-modified signaling molecules
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Saccharomyces cerevisiae
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fusion of ubiquitin to mutant enzyme Ste6p-deltaA dramatically increased its rate of turnover
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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enzyme variant with a deletion in the linker region
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
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1 * 145000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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1 * 145000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
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not glycosylated
phosphoprotein
additional information
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accumulates in the plasma membrane in a ubiquintinated form in endocytosis mutants
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
metabolically unstable in wild-type strain
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the very unstable protein is stabilized approximately 3fold in a ubc4 ubc5 mutant, strongest stabilization in the vacuolar pep4 mutant
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two independent degradative systems, the vacuolar Pep4p-dependent proteases and the cytosolic proteasome are both involved, either directly or indirectly, in the metabolic degradation of the alpha-factor-transporting ATPase
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immunoprecipitation using anti-Ste6 antibodies
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21 (DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A517P
mutant enzyme shows 0.01% of the mating efficiency of the wild-type enzyme
A517T
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mates with wild-type efficiency at 30°C. The organism shows 2-3fold decrease in mating at 37°C
A532H
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mates with wild-type efficiency at 30°C. The organism shows 2-3fold decrease in mating at 37°C
DELTA-Abox
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concurrent loss of phosphorylation and ubiquitination in the A-box mutant
E439K
mutant enzyme shows 0.01% of the mating efficiency of the wild-type enzyme
E531K/V533I
mutant enzyme shows 0.75% of the mating efficiency of the wild-type enzyme
F630L
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mutant shows polar cell surface staining, indistinguishable from wild-type Ste6
F656L
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mutant shows polar cell surface staining, indistinguishable from wild-type Ste6
G1087D
mutant enzyme is completely defective for mating
G1092E
mutant enzyme is completely defective for mating
G320D
mutant enzyme shows 5.5% of the mating efficiency of the wild-type enzyme
G320V
mutant enzyme shows 6% of the mating efficiency of the wild-type enzyme
G38D
mutant enzyme is completly defective for mating, mutant enzyme does not accumulate in plasma membrane fraction
G38N
mutant enzyme shows 0.06-0.01% of the mating efficiency of the wild-type enzyme
G392E
mutant enzyme is completely defective for mating
G392K
mutant enzyme is completely defective for mating
G397D
mutant enzyme is completely defective for mating
G397N
mutant enzyme shows 1.7% of the mating efficiency of the wild-type enzyme
G509D
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significant reduction in alpha-factor transport. The organism shows 56fold decrease in mating relative to wild-type control
I521N
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mates with wild-type efficiency at 30°C. The organism shows 2-3fold decrease in mating at 37°C
P525L
mutant enzyme shows 7% of the mating efficiency of the wild-type enzyme at 25°C, 0.06% at 30°C and is defective for mating at 37°C
R518T
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mates with wild-type efficiency at 30°C. The organism shows 11fold reduction in mating at 37°C
R833K/R941H
mutant enzyme shows 1.9% of the mating efficiency of the wild-type enzyme
S507I
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less severe reduction in alpha-factor transport. The organism shows a mating defect at 30°C
S507N/G508S/G509R
mutant enzyme is completely defective for mating
S507R
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significant reduction in alpha-factor transport. The organism shows a mating defect at 30°C
S623L
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3fold increased stability compared to wild-type enzyme, phosphorylation is reduced
S632F/Q633STOP
mutant enzyme shows 1.8% of the mating efficiency of the wild-type enzyme
T613A
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2fold increased stability compared to wild-type enzyme, phosphorylation is not affected
T613A/S623L
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5fold increased stability compared to wild-type enzyme
Y648L
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mutant shows polar cell surface staining, indistinguishable from wild-type Ste6
Y657L
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mutant shows polar cell surface staining, indistinguishable from wild-type Ste6
Y661L
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mutant shows polar cell surface staining, indistinguishable from wild-type Ste6
Y681L
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Tyr681 is part of the recycling signals in Ste6
Y713L
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mutant shows polar cell surface staining, indistinguishable from wild-type Ste6
DELTA-Abox
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concurrent loss of phosphorylation and ubiquitination in the A-box mutant
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S623L
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3fold increased stability compared to wild-type enzyme, phosphorylation is reduced
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T613A
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2fold increased stability compared to wild-type enzyme, phosphorylation is not affected
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T613A/S623L
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5fold increased stability compared to wild-type enzyme
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