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Information on EC 1.20.2.1 - arsenate reductase (cytochrome c)

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EC Tree
IUBMB Comments
A molybdoprotein containing iron-sulfur clusters. Isolated from alpha-proteobacteria. Unlike EC 1.20.9.1, arsenate reductase (azurin), it does not use azurin as acceptor.
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This record set is specific for:
UNIPROT: Q6VAL9
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
2
oxidized cytochrome c
=
+
2
reduced cytochrome c
+
2
Synonyms
as(iii) oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aroB
arsenite-oxidising bacterium
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
arsenite:cytochrome c oxidoreductase
A molybdoprotein containing iron-sulfur clusters. Isolated from alpha-proteobacteria. Unlike EC 1.20.9.1, arsenate reductase (azurin), it does not use azurin as acceptor.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arsenite + cytochrome c + H2O
arsenate + reduced cytochrome c
show the reaction diagram
arsenite-oxidising bacterium
horse heart cytochrome c serves as an in vitro elelctron acceptor
-
-
?
arsenite + cytochrome c552 + H2O
arsenate + reduced cytochrome c552
show the reaction diagram
arsenite-oxidising bacterium
physiological electron acceptor
-
-
?
arsenite + H2O + 2,6-dichlorophenolindophenol
arsenate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
arsenite-oxidising bacterium
-
-
-
?
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
arsenite + cytochrome c552 + H2O
arsenate + reduced cytochrome c552
show the reaction diagram
arsenite-oxidising bacterium
physiological electron acceptor
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c552
arsenite-oxidising bacterium
physiological electron acceptor to the arsenite oxidase, the gene that encodes this protein is located downstream of the arsenite oxidase genes aroBA. Characterisation reveals the presence of a single heme per protein and that the heme redox potential is similar to that of mitochondrial c-type cytochromes
-
molybdenum cofactor
arsenite-oxidising bacterium
protein contains two molybdenum and 9 or 10 iron atoms per alpha2beta2 unit
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
arsenite-oxidising bacterium
protein contains two molybdenum and 9 or 10 iron atoms per alpha2beta2 unit
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.061
arsenite
arsenite-oxidising bacterium
pH 5.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.6
arsenite
arsenite-oxidising bacterium
pH 5.5, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
arsenite-oxidising bacterium
subunit aroB
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
arsenite-oxidising bacterium
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q6VAL9_9HYPH
175
0
18355
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
arsenite-oxidising bacterium
2 * 98000, subunit aroA, plus 2 * 14000, subunit aroB, SDS-PAGE
219000
arsenite-oxidising bacterium
gel filtration
98000
arsenite-oxidising bacterium
2 * 98000, subunit aroA, plus 2 * 14000, subunit aroB, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
arsenite-oxidising bacterium
2 * 98000, subunit aroA, plus 2 * 14000, subunit aroB, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
-
arsenite-oxidising bacterium
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Santini, J.; Kappler, U.; Ward, S.; Honeychurch, M.; vanden Hoven, R.; Bernhardt, P.
The NT-26 cytochrome c552 and its role in arsenite oxidation
Biochim. Biophys. Acta
1767
189-196
2007
arsenite-oxidising bacterium (Q6VAL9), arsenite-oxidising bacterium NT-26 (Q6VAL9)
Manually annotated by BRENDA team
Santini, J.; Vanden Hoven, R.
Molybdenum-containing arsenite oxidase of the chemolithoautotrophic arsenite oxidizer NT-26
J. Bacteriol.
186
1614-1619
2004
arsenite-oxidising bacterium (Q6VAL9), arsenite-oxidising bacterium NT-26 (Q6VAL9), Pseudorhizobium banfieldiae (Q6VAL8)
Manually annotated by BRENDA team