2-aminoethanethiol dioxygenase [Mus musculus]
cysteine dioxygenase family protein( domain architecture ID 10545174)
cysteine dioxygenase family protein containing a cupin domain, similar to plant cysteine oxidases and mammalian 2-aminoethanethiol dioxygenase (also called cysteamine dioxygenase)
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
PCO_ADO | pfam07847 | PCO_ADO; This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol ... |
45-254 | 2.05e-89 | ||||
PCO_ADO; This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol dioxygenases (ADOs) from animals. : Pssm-ID: 462286 Cd Length: 201 Bit Score: 263.03 E-value: 2.05e-89
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Name | Accession | Description | Interval | E-value | ||||
PCO_ADO | pfam07847 | PCO_ADO; This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol ... |
45-254 | 2.05e-89 | ||||
PCO_ADO; This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol dioxygenases (ADOs) from animals. Pssm-ID: 462286 Cd Length: 201 Bit Score: 263.03 E-value: 2.05e-89
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cupin_ADO | cd20289 | 2-aminoethanethiol dioxygenase, cupin domain; This family contains 2-aminoethanethiol ... |
82-199 | 3.34e-44 | ||||
2-aminoethanethiol dioxygenase, cupin domain; This family contains 2-aminoethanethiol dioxygenase (also known as cysteamine dioxygenase, persulfurase or ADO; EC 1.13.11.19), which catalyzes the addition of two oxygen atoms to free cysteamine (2-aminoethanethiol) to form hypotaurine that subsequently oxidizes to taurine. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380423 Cd Length: 103 Bit Score: 144.62 E-value: 3.34e-44
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Name | Accession | Description | Interval | E-value | ||||
PCO_ADO | pfam07847 | PCO_ADO; This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol ... |
45-254 | 2.05e-89 | ||||
PCO_ADO; This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol dioxygenases (ADOs) from animals. Pssm-ID: 462286 Cd Length: 201 Bit Score: 263.03 E-value: 2.05e-89
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cupin_ADO | cd20289 | 2-aminoethanethiol dioxygenase, cupin domain; This family contains 2-aminoethanethiol ... |
82-199 | 3.34e-44 | ||||
2-aminoethanethiol dioxygenase, cupin domain; This family contains 2-aminoethanethiol dioxygenase (also known as cysteamine dioxygenase, persulfurase or ADO; EC 1.13.11.19), which catalyzes the addition of two oxygen atoms to free cysteamine (2-aminoethanethiol) to form hypotaurine that subsequently oxidizes to taurine. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380423 Cd Length: 103 Bit Score: 144.62 E-value: 3.34e-44
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cupin_CDO | cd10548 | cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ... |
68-132 | 2.99e-05 | ||||
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380416 [Multi-domain] Cd Length: 100 Bit Score: 41.90 E-value: 2.99e-05
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Blast search parameters | ||||
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