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Enzyme Nomenclature
Information on EC 1.14.12.14 - 2-aminobenzenesulfonate 2,3-dioxygenase
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The expected taxonomic range for this enzyme is: Alcaligenes
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EC NUMBER 
COMMENTARY 
1.14.12.14
-
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RECOMMENDED NAME
GeneOntology No.
2-aminobenzenesulfonate 2,3-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminobenzenesulfonate + NADH + H+ + O2 = 2,3-dihydroxybenzenesulfonate + NH3 + NAD+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
2-aminobenzenesulfonate,NADH:oxygen oxidoreductase (2,3-hydroxylating, ammonia-forming)
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CAS REGISTRY NUMBER
COMMENTARY
156621-16-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
AbsAa, enzyme component; DSM 6325, six genes of the abs cluster are co-transcribed and contain the genes for two subunits of the oxygenase component of the ABS-dioxygenase system
UniProt
AbsAb, enzyme component; DSM 6325, six genes of the abs cluster are co-transcribed and contain the genes for two subunits of the oxygenase component of the ABS-dioxygenase system
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
Alcaligenes sp. O-1 inducibly deaminates 2-aminobenzenesulfonate via dioxygenation to 3-sulfocatechol, which is desulfonated during meta ring-cleavage to yield 2-hydroxymuconate. This intermediate is transformed through the oxalocrotonate-branch of the sulfocatechol meta-pathway, overview. The pathway shows both split operons and dispersed pathway genes, and no transcriptional regulator, overview. The overall degradative process for ABS in strain O-1 is complex, overview; Alcaligenes sp. O-1 inducibly deaminates 2-aminobenzenesulfonate via dioxygenation to 3-sulfocatechol, which is desulfonated during meta ring-cleavage to yield 2-hydroxymuconate. This intermediate is transformed through the oxalocrotonate-branch of the sulfocatechol meta-pathway, overview. The pathway shows both split operons and dispersed pathway genes, and no transcriptional regulator, overview. The overall degradative process for ABS in strain O-1 is complex, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-Aminobenzenesulfonate + NADH + H+ + O2
3-Sulfocatechol + NH3 + NAD+
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2-aminobenzenesulfonate + NADH + H+ + O2
2,3-dihydroxybenzenesulfonate + NH3 + NAD+
2-aminobenzenesulfonate is used in the manufacture of dyes and pharmaceuticals, and, typical of xenobiotic aryl-sulfonates. The compound is degraded in few native environments, e.g. by Alcaligenes sp. strain O-1, the overall degradative process for ABS in strain O-1 is complex, overview. The pathway shows both split operons and dispersed pathway genes, and no transcriptional regulator
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?
2-aminobenzenesulfonate + NADH + H+ + O2
2,3-dihydroxybenzenesulfonate + NH3 + NAD+
i.e. orthanilate or ABS
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?
2-aminobenzenesulfonate + NADH + H+ + O2
?
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initial step in degradation of of 2-aminobenzenesulfonate
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2-aminobenzenesulfonate + NADH + H+ + O2
?
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initial step in degradation of of 2-aminobenzenesulfonate
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2-aminobenzenesulfonate + NADH + O2
3-sulfocatechol + NH3 + NAD+
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enables utilization of 2-aminobenzenesulfonate as sole carbon and energy source
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzenesulfonate + NADH + H+ + O2
2,3-dihydroxybenzenesulfonate + NH3 + NAD+
Q9RBG4, Q9RBG5
2-aminobenzenesulfonate is used in the manufacture of dyes and pharmaceuticals, and, typical of xenobiotic aryl-sulfonates. The compound is degraded in few native environments, e.g. by Alcaligenes sp. strain O-1, the overall degradative process for ABS in strain O-1 is complex, overview. The pathway shows both split operons and dispersed pathway genes, and no transcriptional regulator
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-
?
2-aminobenzenesulfonate + NADH + O2
3-sulfocatechol + NH3 + NAD+
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enables utilization of 2-aminobenzenesulfonate as sole carbon and energy source
-
-
?
2-aminobenzenesulfonate + NADH + H+ + O2
?
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initial step in degradation of of 2-aminobenzenesulfonate
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-
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2-aminobenzenesulfonate + NADH + H+ + O2
?
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initial step in degradation of of 2-aminobenzenesulfonate
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
part of the reductive component; part of the reductive component
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme is composed of two components, AbsAa and AbsAb; the enzyme is composed of two components, AbsAa and AbsAb
additional information
the enzyme is composed of two components, AbsAa and AbsAb; the enzyme is composed of two components, AbsAa and AbsAb
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene absAa, DNA and amino acid sequence determination and analysis. Six genes of the abs cluster are co-transcribed and contain the genes, absAa and absAb, for two subunits of the oxygenase component of the ABS-dioxygenase system. Sequence comparisons, overview; gene absAb, DNA and amino acid sequence determination and analysis. Six genes of the abs cluster are co-transcribed and contain the genes, absAa and absAb, for two subunits of the oxygenase component of the ABS-dioxygenase system. Sequence comparisons, overview
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.12.14)
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