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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 7.1.2.1 - P-type H+-exporting transporter

for references in articles please use BRENDA:EC7.1.2.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q9Y487
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide
ATP
+
H2O
+
4
H+[side 1]
=
ADP
+
phosphate
+
4
H+[side 2]
+
+
4
=
+
+
4
Synonyms
plasma membrane atpase, plasma membrane h+-atpase, pm h+-atpase, pma1p, vacuolar proton pump, plasma membrane proton pump, v-h+-atpase, yeast plasma membrane atpase, yeast plasma membrane h+-atpase, p-type h+-atpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
vacuolar-type H+-ATPase
-
ATP phosphohydrolase
-
-
-
-
H+-ATPase
-
-
-
-
LDH1A protein
-
-
-
-
LDH1B protein
-
-
-
-
PAT2
-
-
-
-
Proton pump
-
-
-
-
Proton pump 10
-
-
-
-
Proton pump 11
-
-
-
-
proton-translocating ATPase
-
-
-
-
yeast plasma membrane ATPase
-
-
-
-
yeast plasma membrane H+-ATPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transmembrane transport
-
-
-
-
hydrolysis of phosphate bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (H+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
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 + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
VPP2_HUMAN
856
0
98082
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
recombinant N-terminal cytosolic tail of V-ATPase a2-subunit isoform a2N1-402, NuPAGE
48500
recombinant N-terminal cytosolic tail of V-ATPase a2-subunit isoform a2N1-402, calculated from amino acid sequence
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NDSB-256 is required not only during protein refolding but also afterward for stabilization of a2N1-402 protein in the solution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Talon bead chromatography, HisTrap column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subunit a2N1-402 is expressed in Escherichia coli BL21(DE3) cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
best refolding conditions are 1 M NDSB-256, 1 mM dithiothreitol, 100 mM CHES, and pH 9.0
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Merkulova, M.; McKee, M.; Dip, P.V.; Grueber, G.; Marshansky, V.
N-terminal domain of the V-ATPase a2-subunit displays integral membrane protein properties
Protein Sci.
19
1850-1862
2010
Homo sapiens (Q9Y487)
Manually annotated by BRENDA team