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Information on EC 7.2.2.2 - ABC-type Cd2+ transporter

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EC Tree
IUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports some heavy metals, especially Cd2+, from the cytosol into the vacuole.
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This record set is specific for:
UNIPROT: Q1LAJ7
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ycf1p, oshma3, yor1p, hmt-1, yeast cadmium factor, yeast cadmium factor 1, cadmium-transporting atpase, hmt1 protein, heavy metal-associated atpase, heavy metal tolerance factor 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP phosphohydrolase (heavy-metal-exporting)
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cadmium-transporting ATPase
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yeast cadmium factor
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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transmembrane transport
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, heavy-metal-exporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports some heavy metals, especially Cd2+, from the cytosol into the vacuole.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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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 + H2O + Cd2+[side 1]
ADP + phosphate + Cd2+[side 2]
show the reaction diagram
highest activity
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?
ATP + H2O + Co2+[side 1]
ADP + phosphate + Co2+[side 2]
show the reaction diagram
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?
ATP + H2O + Zn2+[side 1]
ADP + phosphate + Zn2+[side 2]
show the reaction diagram
lowest activity
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Cd2+[side 1]
ADP + phosphate + Cd2+[side 2]
show the reaction diagram
highest activity
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?
ATP + H2O + Co2+[side 1]
ADP + phosphate + Co2+[side 2]
show the reaction diagram
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?
ATP + H2O + Zn2+[side 1]
ADP + phosphate + Zn2+[side 2]
show the reaction diagram
lowest activity
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?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
with Cd2+ as transport ion, at pH 7.5 and 30°C
0.06
with Co2+ as transport ion, at pH 7.5 and 30°C
0.2
with Cd2+ as transport ion, at pH 7.5 and 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly named Alcaligenes eutrophus and Ralstonia metallidurans
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q1LAJ7_CUPMC
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
829
0
86994
TrEMBL
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C476A
the mutant enzyme binds 0.61 mol equiv of Co2+. The mutant enzyme shows about 4%, about 24%, and about 30% of Cd2+-, Co2+-, and Zn2+-stimulated ATP hydrolysis activity, respectively, compared to the wild type enzyme
H807A
the mutant enzyme retains the ability to bind about 1 mol equiv of all metal ions (Co2+, Zn2+, and Cd2+). The mutation results in a strong decrease in Co2+- (about 17% of wild type) and Zn2+-stimulated (about 16% of wild type) ATP hydrolysis
M254A
the mutant enzyme binds 0.34 mol and 0.26 mol equiv of Cd2+ and Co2+, respectively. The mutation dramatically reduces Cd2+- and Co2+-stimulated ATPase activity (about 8% and about 32% of wild type activity, respectively), whereas Zn2+-stimulated ATPase activity remains virtually unchanged
S474A
the mutant enzyme binds 0.45 mol equiv of Co2+. The mutation modestly decreases Co2+-stimulated ATP hydrolysis (about 66% of wild type activity) whereas Cd2+- and Zn2+-stimulated ATP hydrolysis remain virtually unchanged
S474A/C476A
the mutant enzyme shows about 2%, about 16%, and about 20% of Cd2+-, Co2+-, and Zn2+-stimulated ATP hydrolysis activity, respectively, compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-charged HiTrap column chromatography and Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Smith, A.T.; Ross, M.O.; Hoffman, B.M.; Rosenzweig, A.C.
Metal selectivity of a Cd-, Co-, and Zn-transporting P1B-type ATPase
Biochemistry
56
85-95
2017
Cupriavidus metallidurans (Q1LAJ7)
Manually annotated by BRENDA team