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Information on EC 1.20.9.1 - arsenate reductase (azurin) and Organism(s) Alcaligenes faecalis and UniProt Accession Q7SIF3

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IUBMB Comments
Contains a molybdopterin centre comprising two molybdopterin guanosine dinucleotide cofactors bound to molybdenum, a [3Fe-4S] cluster and a Rieske-type [2Fe-2S] cluster. Isolated from beta-proteobacteria. Also uses a c-type cytochrome or O2 as acceptors.
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This record set is specific for:
Alcaligenes faecalis
UNIPROT: Q7SIF3
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The taxonomic range for the selected organisms is: Alcaligenes faecalis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
+
+
2
oxidized azurin
=
+
2
+
2
Synonyms
arsenite oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
arsenite oxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
arsenite:azurin oxidoreductase
Contains a molybdopterin centre comprising two molybdopterin guanosine dinucleotide cofactors bound to molybdenum, a [3Fe-4S] cluster and a Rieske-type [2Fe-2S] cluster. Isolated from beta-proteobacteria. Also uses a c-type cytochrome or O2 as acceptors.
CAS REGISTRY NUMBER
COMMENTARY hide
144638-82-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arsenite + H2O + azurin(oxidized)
arsenate + azurin(reduced)
show the reaction diagram
additional information
?
-
-
enzyme is expressed during the exponential and stationary phases of growth. Arsenite oxidase, azurin and cytochrome c may form the basis of an electron transport chain
-
-
?
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
additional information
?
-
-
enzyme is expressed during the exponential and stationary phases of growth. Arsenite oxidase, azurin and cytochrome c may form the basis of an electron transport chain
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iron-sulfur centre
the large subunit contains a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site
iron-sulfur centre
the large subunit contains a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site
molybdopterin
the large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
the large subunit contains a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site
Iron
the large subunit contains a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site
Molybdenum
the large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
arsenite
-
-
0.008
azurin
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
small subunit aoxA
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
enzyme is expressed during the exponential and stationary phases of growth
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AIOB_ALCFA
175
0
18275
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
SDS-PAGE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of arsenite oxidase to 2.03A in a P21 crystal form with two molecules in the asymmetric unit and to 1.64 A in a P1 crystal form with four molecules in the asymmetric unit. The large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors, and a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site
crystal structure of arsenite oxidase to 2.03A in a P21 crystal form with two molecules in the asymmetric unit and to 1.64 A in a P1 crystal form with four molecules in the asymmetric unit. The large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors, and a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
-
important implications for biomediation of arsenite contaminated soils and groud water
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anderson, G.L.; Williams, J.; Hille, R.
The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase
J. Biol. Chem.
267
23674-23682
1992
Alcaligenes faecalis
Manually annotated by BRENDA team
Ellis, P.J.; Conrads, T.; Hille, R.; Kuhn, P.
Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A
Structure
9
125-132
2001
Alcaligenes faecalis, Alcaligenes faecalis (Q7SIF3), Alcaligenes faecalis (Q7SIF4), Alcaligenes faecalis NCIB 8687 (Q7SIF3), Alcaligenes faecalis NCIB 8687 (Q7SIF4), Alcaligenes faecalis NCIB 8687
Manually annotated by BRENDA team
Anderson, G.L.; Love, M.; Zeider, B.K.
Metabolic energy from arsenite oxidation in Alcaligenes faecalis
J. Phys. IV Proc.
107
49-52
2003
Alcaligenes faecalis
-
Manually annotated by BRENDA team