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Literature summary extracted from

  • Cheng, N.; Paris, V.; Rao, X.; Wang, X.; Nakata, P.A.
    A conserved oxalyl-coenzyme A decarboxylase in oxalate catabolism (2022), Plant Signal. Behav., 17, 2062555.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Arabidopsis thaliana
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Danio rerio
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Escherichia coli
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Glycine max
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Homo sapiens
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Hordeum vulgare
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Medicago truncatula
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Mus musculus
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Oryza sativa
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Oxalobacter formigenes
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Saccharomyces cerevisiae
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Solanum lycopersicum
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Triticum aestivum
4.1.1.8 OXC, sequence comparisons and phylogenetic analysis Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.8 Oxalyl-CoA Oryza sativa
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Triticum aestivum
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Hordeum vulgare
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Solanum lycopersicum
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Medicago truncatula
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Glycine max
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Oxalobacter formigenes
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Escherichia coli
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Arabidopsis thaliana
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Saccharomyces cerevisiae
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Danio rerio
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Mus musculus
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Homo sapiens
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Zea mays
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Escherichia coli K12
-
 Formyl-CoA + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.8 Arabidopsis thaliana
-
-
-
4.1.1.8 Danio rerio
-
-
-
4.1.1.8 Escherichia coli P0AFI0
-
-
4.1.1.8 Escherichia coli K12 P0AFI0
-
-
4.1.1.8 Glycine max
-
-
-
4.1.1.8 Homo sapiens
-
-
-
4.1.1.8 Hordeum vulgare
-
-
-
4.1.1.8 Medicago truncatula
-
-
-
4.1.1.8 Mus musculus
-
-
-
4.1.1.8 Oryza sativa
-
-
-
4.1.1.8 Oxalobacter formigenes P40149
-
-
4.1.1.8 Saccharomyces cerevisiae
-
-
-
4.1.1.8 Solanum lycopersicum
-
-
-
4.1.1.8 Triticum aestivum
-
-
-
4.1.1.8 Zea mays
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.8 Oxalyl-CoA
-
 Oryza sativa Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Triticum aestivum Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Hordeum vulgare Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Solanum lycopersicum Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Medicago truncatula Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Glycine max Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Oxalobacter formigenes Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Escherichia coli Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Arabidopsis thaliana Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Saccharomyces cerevisiae Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Danio rerio Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Mus musculus Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Homo sapiens Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Zea mays Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Escherichia coli K12 Formyl-CoA + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Oryza sativa
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Triticum aestivum
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Hordeum vulgare
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Solanum lycopersicum
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Medicago truncatula
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Glycine max
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Oxalobacter formigenes
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Escherichia coli
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Arabidopsis thaliana
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Saccharomyces cerevisiae
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Danio rerio
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Mus musculus
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Homo sapiens
4.1.1.8 additional information OXCs have three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Zea mays

Synonyms

EC Number Synonyms Comment Organism
4.1.1.8 AtOXC
-
 Arabidopsis thaliana
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Oryza sativa
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Triticum aestivum
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Hordeum vulgare
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Solanum lycopersicum
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Medicago truncatula
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Glycine max
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Oxalobacter formigenes
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Escherichia coli
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Arabidopsis thaliana
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Saccharomyces cerevisiae
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Danio rerio
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Mus musculus
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Homo sapiens
4.1.1.8 oxalyl-coenzyme A decarboxylase
-
 Zea mays
4.1.1.8 OXC
-
 Oryza sativa
4.1.1.8 OXC
-
 Triticum aestivum
4.1.1.8 OXC
-
 Hordeum vulgare
4.1.1.8 OXC
-
 Solanum lycopersicum
4.1.1.8 OXC
-
 Medicago truncatula
4.1.1.8 OXC
-
 Glycine max
4.1.1.8 OXC
-
 Oxalobacter formigenes
4.1.1.8 OXC
-
 Escherichia coli
4.1.1.8 OXC
-
 Arabidopsis thaliana
4.1.1.8 OXC
-
 Saccharomyces cerevisiae
4.1.1.8 OXC
-
 Danio rerio
4.1.1.8 OXC
-
 Mus musculus
4.1.1.8 OXC
-
 Homo sapiens
4.1.1.8 OXC
-
 Zea mays
4.1.1.8 ScOXC
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.8 thiamine diphosphate dependent on Oryza sativa
4.1.1.8 thiamine diphosphate dependent on Triticum aestivum
4.1.1.8 thiamine diphosphate dependent on Hordeum vulgare
4.1.1.8 thiamine diphosphate dependent on Solanum lycopersicum
4.1.1.8 thiamine diphosphate dependent on Medicago truncatula
4.1.1.8 thiamine diphosphate dependent on Glycine max
4.1.1.8 thiamine diphosphate dependent on Oxalobacter formigenes
4.1.1.8 thiamine diphosphate dependent on Escherichia coli
4.1.1.8 thiamine diphosphate dependent on Arabidopsis thaliana
4.1.1.8 thiamine diphosphate dependent on Saccharomyces cerevisiae
4.1.1.8 thiamine diphosphate dependent on Danio rerio
4.1.1.8 thiamine diphosphate dependent on Mus musculus
4.1.1.8 thiamine diphosphate dependent on Homo sapiens
4.1.1.8 thiamine diphosphate dependent on Zea mays

General Information

EC Number General Information Comment Organism
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Oryza sativa
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Triticum aestivum
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Hordeum vulgare
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Solanum lycopersicum
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Medicago truncatula
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Glycine max
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Oxalobacter formigenes
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Escherichia coli
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Arabidopsis thaliana
4.1.1.8 evolution phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain Zea mays
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Oryza sativa
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Triticum aestivum
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Hordeum vulgare
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Solanum lycopersicum
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Medicago truncatula
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Glycine max
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Oxalobacter formigenes
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Escherichia coli
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Arabidopsis thaliana
4.1.1.8 metabolism the enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Saccharomyces cerevisiae
4.1.1.8 metabolism the enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Danio rerio
4.1.1.8 metabolism the enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Mus musculus
4.1.1.8 metabolism the enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Homo sapiens
4.1.1.8 metabolism the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants Zea mays
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Oryza sativa
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Triticum aestivum
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Hordeum vulgare
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Solanum lycopersicum
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Medicago truncatula
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Glycine max
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Oxalobacter formigenes
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Escherichia coli
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Arabidopsis thaliana
4.1.1.8 physiological function the ability to biosynthesize oxalic acid can provide beneficial functions to plants, but uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. The enzyme catalyzes the second step in the CoA-dependent pathway of oxalate degradation Zea mays