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Information on EC 7.3.2.7 - arsenite-transporting ATPase and Organism(s) Homo sapiens and UniProt Accession O43681

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IUBMB Comments
This bacterial transporter does not belong to the ABC superfamily, and instead is a member of its own family, referred to as the Ars family. The enzyme usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. It forms an arsenite efflux pump that removes arsenite from the cytoplasm, and can also remove antimonite anions.
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This record set is specific for:
Homo sapiens
UNIPROT: O43681
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Word Map
  • 7.3.2.7
  • metalloid
  • sbiii
  • tail-anchored
  • antimonials
  • arsd
  • metallochaperone
  • oxyanions
  • trivalent
  • oxyanion-translocating
  • anion-translocating
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
asna1, arsa atpase, asna-1, arsab, arsab pump, giarsa, arsab extrusion pump, arsab as(iii) efflux pump, riarsb, arsenite-translocating atpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ARSA
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-
-
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Arsenical resistance ATPase
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-
-
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Arsenite-translocating ATPase
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-
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Arsenite-transporting ATPase
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ATP-dependent arsenite pump
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (arsenite-exporting)
This bacterial transporter does not belong to the ABC superfamily, and instead is a member of its own family, referred to as the Ars family. The enzyme usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. It forms an arsenite efflux pump that removes arsenite from the cytoplasm, and can also remove antimonite anions.
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 + arsenite/in
ADP + phosphate + arsenite/out
show the reaction diagram
-
-
-
?
ATP + H2O + cisplatin/in
ADP + phosphate + cisplatin/out
show the reaction diagram
-
-
-
?
additional information
?
-
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 + arsenite/in
ADP + phosphate + arsenite/out
show the reaction diagram
-
-
-
?
ATP + H2O + cisplatin/in
ADP + phosphate + cisplatin/out
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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?
GET3_HUMAN
348
0
38793
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transfection of T-289 melanoma cells with either ASNA1 sense or ASNA1 antisense constructs, expression analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hemmingsson, O.; Zhang, Y.; Still, M.; Naredi, P.
ASNA1, an ATPase targeting tail-anchored proteins, regulates melanoma cell growth and sensitivity to cisplatin and arsenite
Cancer Chemother. Pharmacol.
63
491-499
2009
Homo sapiens (O43681), Homo sapiens
Manually annotated by BRENDA team