1.1.1.179 D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming) oxidation - Macaca fascicularis Q9TQS6 1.1.1.213 3alpha-hydroxysteroid 3-dehydrogenase (Re-specific) oxidation - Rattus norvegicus P23457 1.1.1.219 dihydroflavonol 4-reductase oxidation - Fragaria x ananassa - 1.1.1.223 isopiperitenol dehydrogenase oxidation - Mentha x piperita - 1.1.1.24 quinate/shikimate dehydrogenase (NAD+) oxidation - Actinidia arguta - 1.1.1.24 quinate/shikimate dehydrogenase (NAD+) oxidation - Actinidia chinensis - 1.1.1.24 quinate/shikimate dehydrogenase (NAD+) oxidation - Actinidia deliciosa - 1.1.1.243 carveol dehydrogenase oxidation - Mentha spicata - 1.1.1.263 1,5-anhydro-D-fructose reductase oxidation - Ensifer adhaerens - 1.1.1.281 GDP-4-dehydro-6-deoxy-D-mannose reductase oxidation - Aneurinibacillus thermoaerophilus Q6T1X6 1.1.1.284 S-(hydroxymethyl)glutathione dehydrogenase oxidation - Homo sapiens - 1.1.1.290 4-phosphoerythronate dehydrogenase oxidation - Escherichia coli P05459 1.1.1.36 acetoacetyl-CoA reductase oxidation - Rattus norvegicus - 1.1.1.49 glucose-6-phosphate dehydrogenase (NADP+) oxidation - Fragaria x ananassa - 1.1.1.51 3(or 17)beta-hydroxysteroid dehydrogenase oxidation - Homo sapiens - 1.1.1.67 mannitol 2-dehydrogenase oxidation oxidation of D-mannitol Leuconostoc pseudomesenteroides - 1.1.1.67 mannitol 2-dehydrogenase oxidation oxidation of D-sorbitol Gluconobacter oxydans - 1.1.1.B18 L-1-amino-2-propanol dehydrogenase oxidation - Rhodococcus erythropolis A1IG83 1.1.1.B20 meso-2,3-butandiol dehydrogenase oxidation - Klebsiella pneumoniae - 1.1.1.B40 11beta-hydroxysteroid dehydrogenase (NAD+) oxidation - Homo sapiens P80365 1.1.3.10 pyranose oxidase oxidation C2-oxidation Coriolus sp. - 1.1.3.16 ecdysone oxidase oxidation - Drosophila melanogaster - 1.1.3.42 prosolanapyrone-II oxidase oxidation - Alternaria solani - 1.1.3.6 cholesterol oxidase oxidation - Streptomyces sp. P12676 1.1.5.13 (S)-2-hydroxyglutarate dehydrogenase oxidation - Escherichia coli - 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) oxidation - Acinetobacter calcoaceticus P13650 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) oxidation - Escherichia coli - 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) oxidation - Streptomyces coelicolor - 1.1.5.5 alcohol dehydrogenase (quinone) oxidation - Acidomonas methanolica - 1.1.7.1 4-hydroxybenzoyl-CoA reductase oxidation - Thauera aromatica - 1.1.99.13 glucoside 3-dehydrogenase (acceptor) oxidation oxidation of the C-3 hydroxyl group of the glucosides and converting them to corresponding 3-ketoglucosides. The Enzyme acts on D-Glucose, D-galactose, D-glycosides and galactosides Stenotrophomonas maltophilia - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Aspergillus fumigatus Q4WZA6 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Aspergillus nidulans - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Athelia rolfsii Q7Z975 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Chaetomium sp. - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Coniophora puteana Q6BDD5 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Flammulina velutipes - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Fusarium graminearum - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Ganoderma gibbosum - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Grifola frondosa Q8J2T4 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Hericium erinaceus - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Heterobasidion annosum - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Humicola insolens Q9P8H5 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Irpex lacteus Q6AW20 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Monilia sp. - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Neurospora crassa - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Phanerodontia chrysosporium Q01738 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Pyricularia grisea - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Saccharomyces cerevisiae - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Schizophyllum commune - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Shewanella frigidimarina - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Thermothelomyces fergusii - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Thermothelomyces myriococcoides - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Trametes cinnabarina O74253 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Trametes hirsuta - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Trametes pubescens - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Trametes versicolor O42729 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - Trametes villosa - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - [Sclerotium] coffeicola - 1.1.99.18 cellobiose dehydrogenase (acceptor) oxidation - [Sclerotium] delphinii - 1.1.99.2 L-2-hydroxyglutarate dehydrogenase oxidation - Homo sapiens Q9H9P8 1.1.99.21 D-sorbitol dehydrogenase (acceptor) oxidation - Gluconobacter oxydans - 1.1.99.3 gluconate 2-dehydrogenase (acceptor) oxidation - Campylobacter jejuni Q0PB96 and Q0PB95 1.1.99.3 gluconate 2-dehydrogenase (acceptor) oxidation - Gluconobacter frateurii - 1.1.99.3 gluconate 2-dehydrogenase (acceptor) oxidation - Gluconobacter sp. - 1.1.99.30 2-oxo-acid reductase oxidation - Proteus vulgaris - 1.1.99.31 (S)-mandelate dehydrogenase oxidation - Acinetobacter calcoaceticus - 1.1.99.32 L-sorbose 1-dehydrogenase oxidation - Gluconobacter oxydans - 1.10.5.1 ribosyldihydronicotinamide dehydrogenase (quinone) oxidation - Bos taurus - 1.11.1.1 NADH peroxidase oxidation - Clostridium acetobutylicum Q97D83 1.11.1.1 NADH peroxidase oxidation - Vigna unguiculata - 1.11.1.10 chloride peroxidase oxidation - Leptoxyphium fumago - 1.11.1.11 L-ascorbate peroxidase oxidation - Arabidopsis thaliana - 1.11.1.11 L-ascorbate peroxidase oxidation - Cenchrus americanus A4ZYP9 1.11.1.11 L-ascorbate peroxidase oxidation - Cyanidioschyzon merolae - 1.11.1.11 L-ascorbate peroxidase oxidation - Embryophyta - 1.11.1.11 L-ascorbate peroxidase oxidation - Gossypium hirsutum A7KIX5, C6ZDA9, C6ZDB0, Q39780 1.11.1.11 L-ascorbate peroxidase oxidation - Hordeum vulgare - 1.11.1.11 L-ascorbate peroxidase oxidation - Leishmania major - 1.11.1.11 L-ascorbate peroxidase oxidation - Oryza sativa - 1.11.1.11 L-ascorbate peroxidase oxidation - Populus tomentosa Q5S1V5 1.11.1.11 L-ascorbate peroxidase oxidation - Saccharomyces cerevisiae - 1.11.1.11 L-ascorbate peroxidase oxidation - Solanum lycopersicum Q09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88 1.11.1.11 L-ascorbate peroxidase oxidation - Solanum pennellii - 1.11.1.11 L-ascorbate peroxidase oxidation - Stylosanthes guianensis - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - animal - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Bombus ignitus C3VVL8 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Bos taurus - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Cyprinus carpio - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Homo sapiens - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Momordica charantia Q8W259 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Mus musculus - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Oryza sativa - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Rattus norvegicus - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Saccharomyces cerevisiae - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Schistosoma mansoni - 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase oxidation - Taiwanofungus camphoratus B8K1J5 1.11.1.13 manganese peroxidase oxidation - Basidiomycota - 1.11.1.13 manganese peroxidase oxidation - Bjerkandera adusta - 1.11.1.13 manganese peroxidase oxidation - Cerrena unicolor - 1.11.1.13 manganese peroxidase oxidation - Dichomitus squalens - 1.11.1.13 manganese peroxidase oxidation - Fomes fomentarius - 1.11.1.13 manganese peroxidase oxidation - Gelatoporia subvermispora - 1.11.1.13 manganese peroxidase oxidation - Lentinula edodes B5U990 1.11.1.13 manganese peroxidase oxidation - Lentinus tigrinus - 1.11.1.13 manganese peroxidase oxidation - Phanerodontia chrysosporium Q02567 1.11.1.13 manganese peroxidase oxidation - Trametes maxima - 1.11.1.13 manganese peroxidase oxidation - Trametes ochracea - 1.11.1.13 manganese peroxidase oxidation - Trametes pubescens - 1.11.1.13 manganese peroxidase oxidation - Trametes versicolor - 1.11.1.13 manganese peroxidase oxidation - Trichaptum biforme - 1.11.1.2 NADPH peroxidase oxidation - Desulfovibrio desulfuricans - 1.11.1.2 NADPH peroxidase oxidation - Treponema primitia - 1.11.2.4 fatty-acid peroxygenase oxidation - Bacillus subtilis O31440 1.13.11.1 catechol 1,2-dioxygenase oxidation - Pseudomonas putida - 1.13.11.12 linoleate 13S-lipoxygenase oxidation - Cucumis sativus - 1.13.11.2 catechol 2,3-dioxygenase oxidation - Pseudomonas putida - 1.13.11.34 arachidonate 5-lipoxygenase oxidation the enzyme catalyzes the formation of 5(S)-hydroperoxy-6-trans-8,11,14-cis-eicosatetraenoic acid, 5(S)-hydroxy-6-trans-8,11,14-cis-eicosatetraenoic acid, and 5(S)-trans-5,6-oxido-7,9-trans-11,14-cis eicosatetraenoic acid Homo sapiens - 1.13.11.45 linoleate 11-lipoxygenase oxidation possesses also 1% of hydroperoxide isomerase activity Gaeumannomyces graminis Q8X151 1.13.11.50 acetylacetone-cleaving enzyme oxidation - Acinetobacter johnsonii - 1.13.11.53 acireductone dioxygenase (Ni2+-requiring) oxidation ARD (Ni) converts aci-reductone to 3-(methylthio)propanoate, carbon monoxide, and formate, and the reaction is not part of the methionine salvage pathway cycle (off-pathway). Homo sapiens - 1.13.11.53 acireductone dioxygenase (Ni2+-requiring) oxidation if Ni+2 is bound in the active site, the substrate acireductone reacts with O2 to yield formate and 4-methylthio-2-ketobutyrate Mus musculus - 1.13.11.54 acireductone dioxygenase [iron(II)-requiring] oxidation ARD (Fe), converts the substrate to formate and a keto-acid precursor of methionine that is then converted to methionine (on-pathway) Homo sapiens - 1.13.11.54 acireductone dioxygenase [iron(II)-requiring] oxidation ARD (Fe), converts the substrate to formate and a keto-acid precursor of methionine that is then converted to methionine (on-pathway) Saccharomyces cerevisiae - 1.13.11.54 acireductone dioxygenase [iron(II)-requiring] oxidation if Fe+2 is bound in the active site, the substrate acireductone reacts with O2 to yield formate and 3-(methylthio)propanoate Mus musculus Q99JT9 1.13.11.55 sulfur oxygenase/reductase oxidation - Acidianus tengchongensis Q977W3 1.13.11.63 beta-carotene 15,15'-dioxygenase oxidation - Drosophila melanogaster Q9VFS2 1.13.11.63 beta-carotene 15,15'-dioxygenase oxidation - Galleria mellonella - 1.13.11.63 beta-carotene 15,15'-dioxygenase oxidation - Gallus gallus Q9I993 1.13.11.63 beta-carotene 15,15'-dioxygenase oxidation - Homo sapiens Q9HAY6, Q9HAY6, Q9HAY6 1.13.11.63 beta-carotene 15,15'-dioxygenase oxidation - Mus musculus Q9JJS6 1.13.11.63 beta-carotene 15,15'-dioxygenase oxidation - Rattus norvegicus - 1.13.12.5 Renilla-type luciferase oxidation - Gaussia princeps - 1.13.12.7 firefly luciferase oxidation - Luciola cruciata P13129 1.13.12.7 firefly luciferase oxidation - Luciola mingrelica - 1.13.12.7 firefly luciferase oxidation - Photinus pyralis P08659, P08659, P08659 1.13.99.1 inositol oxygenase oxidation four-electron oxidation of myo-inositol to D-glucuronate Mus musculus - 1.14.11.13 gibberellin 2beta-dioxygenase oxidation - Vigna angularis - 1.14.12.12 naphthalene 1,2-dioxygenase oxidation naphthalene dioxygenase has a relaxed substrate specificity and can oxidize almost 100 substrates, these include the enantiospecific cis-dihydroxylation of polycyclic aromatic hydrocarbons and the olefin groups of benzocycloalkenes, benzylic hydroxylation, N- and O-dealkylation, sulfoxidation and desaturation reactions Pseudomonas sp. - 1.14.12.17 nitric oxide dioxygenase oxidation - Cereibacter sphaeroides - 1.14.12.17 nitric oxide dioxygenase oxidation - Cupriavidus necator P39662 1.14.12.17 nitric oxide dioxygenase oxidation - Escherichia coli P24232 1.14.12.17 nitric oxide dioxygenase oxidation - Mammalia - 1.14.12.17 nitric oxide dioxygenase oxidation - Saccharomyces cerevisiae - 1.14.12.17 nitric oxide dioxygenase oxidation - Vitreoscilla - 1.14.13.101 senecionine N-oxygenase oxidation - Tyria jacobaeae Q8MP06 1.14.13.148 trimethylamine monooxygenase oxidation - Canis lupus familiaris - 1.14.13.148 trimethylamine monooxygenase oxidation - Homo sapiens - 1.14.13.170 pentalenolactone D synthase oxidation Baeyer-Villiger oxidation Streptomyces arenae - 1.14.13.170 pentalenolactone D synthase oxidation Baeyer-Villiger oxidation Streptomyces exfoliatus - 1.14.13.25 methane monooxygenase (soluble) oxidation - Methylosinus trichosporium - 1.14.13.84 4-hydroxyacetophenone monooxygenase oxidation - Pseudomonas putida - 1.14.14.10 nitrilotriacetate monooxygenase oxidation - Aminobacter aminovorans P54989 1.14.14.120 dammarenediol 12-hydroxylase oxidation - Panax ginseng - 1.14.14.135 glyceollin synthase oxidation - Glycine max - 1.14.14.138 lithocholate 6beta-hydroxylase oxidation - Mesocricetus auratus - 1.14.14.139 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase oxidation - Homo sapiens - 1.14.14.139 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase oxidation - Oryctolagus cuniculus - 1.14.14.162 flavanone 2-hydroxylase oxidation - Glycyrrhiza echinata - 1.14.14.176 taxadiene 5alpha-hydroxylase oxidation - Taxus cuspidata Q6WG30 1.14.14.25 cholesterol 24-hydroxylase oxidation - Homo sapiens - 1.14.14.26 24-hydroxycholesterol 7alpha-hydroxylase oxidation - Mus musculus Q9JKJ9 1.14.14.29 25/26-hydroxycholesterol 7alpha-hydroxylase oxidation - Sus scrofa - 1.14.15.14 methyl-branched lipid omega-hydroxylase oxidation - Mycobacterium tuberculosis P9WPP3 1.14.15.21 zeaxanthin epoxidase oxidation - Solanum lycopersicum P93236 1.14.15.32 pentalenene oxygenase oxidation - Streptomyces avermitilis - 1.14.15.7 choline monooxygenase oxidation - Atriplex hortensis Q9LKN0 1.14.15.7 choline monooxygenase oxidation - Beta vulgaris - 1.14.15.7 choline monooxygenase oxidation - Bienertia sinuspersici - 1.14.15.7 choline monooxygenase oxidation - Suaeda aralocaspica - 1.14.16.1 phenylalanine 4-monooxygenase oxidation - Homo sapiens P00439 1.14.16.1 phenylalanine 4-monooxygenase oxidation S-oxidation of S-carboxymethyl-L-cysteine, C-oxidation of L-phenylalanine Homo sapiens - 1.14.16.2 tyrosine 3-monooxygenase oxidation - Rattus norvegicus - 1.14.17.3 peptidylglycine monooxygenase oxidation - Blattella germanica - 1.14.17.3 peptidylglycine monooxygenase oxidation - Homo sapiens - 1.14.17.3 peptidylglycine monooxygenase oxidation - Rattus norvegicus P14925 1.14.17.4 aminocyclopropanecarboxylate oxidase oxidation - Malus domestica O48882, Q00985 1.14.17.4 aminocyclopropanecarboxylate oxidase oxidation - Malus sylvestris - 1.14.17.4 aminocyclopropanecarboxylate oxidase oxidation - Morus alba Q0PNH5 1.14.17.4 aminocyclopropanecarboxylate oxidase oxidation - Nicotiana suaveolens Q069K4 1.14.17.4 aminocyclopropanecarboxylate oxidase oxidation - Zea mays - 1.14.18.2 CMP-N-acetylneuraminate monooxygenase oxidation - Homo sapiens C1K3L2 1.14.19.2 stearoyl-[acyl-carrier-protein] 9-desaturase oxidation - Arabidopsis thaliana O22832 1.14.19.2 stearoyl-[acyl-carrier-protein] 9-desaturase oxidation - Cinnamomum longipaniculatum A8D2K7 1.14.19.20 DELTA7-sterol 5(6)-desaturase oxidation - Arabidopsis thaliana Q39208 1.14.19.20 DELTA7-sterol 5(6)-desaturase oxidation - Tetrahymena thermophila C4PFX1 1.14.19.22 acyl-lipid omega-6 desaturase (cytochrome b5) oxidation - Helianthus annuus O24499 1.14.19.22 acyl-lipid omega-6 desaturase (cytochrome b5) oxidation - Olea europaea A9UKE1, Q4QWZ0, Q4QWZ1 1.14.19.4 acyl-lipid (11-3)-desaturase oxidation - Candida albicans - 1.14.19.4 acyl-lipid (11-3)-desaturase oxidation - Papio anubis B8R1K0 1.14.19.5 acyl-CoA 11-(Z)-desaturase oxidation - Lampronia capitella B6CBS5 1.14.19.5 acyl-CoA 11-(Z)-desaturase oxidation - Ostrinia furnacalis - 1.14.19.5 acyl-CoA 11-(Z)-desaturase oxidation - Ostrinia scapulalis Q2V0N6 1.14.19.65 (S)-cheilanthifoline synthase oxidation - Eschscholzia californica - 1.14.19.67 salutaridine synthase oxidation - Papaver somniferum B1NF18 1.14.19.9 tryptophan 7-halogenase oxidation - Lentzea aerocolonigenes Q8KHZ8 1.14.99.1 prostaglandin-endoperoxide synthase oxidation - Homo sapiens P23219, P35354, P35354 1.14.99.1 prostaglandin-endoperoxide synthase oxidation - Mus musculus - 1.14.99.1 prostaglandin-endoperoxide synthase oxidation - Ovis aries P05979, P79208, P05979, P79208, P05979 1.14.99.1 prostaglandin-endoperoxide synthase oxidation - Rattus norvegicus - 1.14.99.1 prostaglandin-endoperoxide synthase oxidation - Salvelinus fontinalis Q9PTN3, Q9PW89 1.14.99.15 4-methoxybenzoate monooxygenase (O-demethylating) oxidation - Rhodopseudomonas palustris - 1.14.99.22 ecdysone 20-monooxygenase oxidation - Bombyx mori Q3LFR2 1.14.99.22 ecdysone 20-monooxygenase oxidation - Drosophila melanogaster - 1.14.99.22 ecdysone 20-monooxygenase oxidation - Drosophila virilis - 1.14.99.29 deoxyhypusine monooxygenase oxidation - Drosophila melanogaster - 1.14.99.29 deoxyhypusine monooxygenase oxidation - Homo sapiens - 1.14.99.29 deoxyhypusine monooxygenase oxidation - Plasmodium falciparum C9QNK6 1.14.99.29 deoxyhypusine monooxygenase oxidation - Saccharomyces cerevisiae - 1.14.99.38 cholesterol 25-monooxygenase oxidation - Homo sapiens - 1.14.99.38 cholesterol 25-monooxygenase oxidation - Mus musculus Q9Z0F5 1.17.1.5 nicotinate dehydrogenase oxidation - Alcaligenes faecalis - 1.17.3.3 6-hydroxynicotinate dehydrogenase oxidation - Neobacillus niacini - 1.17.5.1 phenylacetyl-CoA dehydrogenase oxidation alpha-oxidation, anaerobic Thauera aromatica - 1.17.99.3 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase oxidation - Rattus norvegicus P97562 1.17.99.4 uracil/thymine dehydrogenase oxidation - Rhodococcus erythropolis - 1.2.1.10 acetaldehyde dehydrogenase (acetylating) oxidation - Acinetobacter sp. HBS-2 A5JT11 1.2.1.11 aspartate-semialdehyde dehydrogenase oxidation - Lactiplantibacillus plantarum - 1.2.1.11 aspartate-semialdehyde dehydrogenase oxidation - Streptococcus pneumoniae - 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) oxidation - Arabidopsis thaliana - 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) oxidation - Homo sapiens P04406 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) oxidation - Kluyveromyces marxianus - 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) oxidation - Oryctolagus cuniculus - 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) oxidation - Spinacia oleracea - 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) oxidation - Chlamydomonas reinhardtii - 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) oxidation - Pisum sativum - 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) oxidation - Spinacia oleracea P19866 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) oxidation - Synechococcus elongatus PCC 7942 = FACHB-805 - 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) oxidation - Triticum aestivum - 1.2.1.16 succinate-semialdehyde dehydrogenase [NAD(P)+] oxidation - Pseudomonas putida - 1.2.1.27 methylmalonate-semialdehyde dehydrogenase (CoA-acylating) oxidation - Oryza sativa Q6Z4E4 1.2.1.28 benzaldehyde dehydrogenase (NAD+) oxidation - Antirrhinum majus - 1.2.1.28 benzaldehyde dehydrogenase (NAD+) oxidation - Sorbus aucuparia - 1.2.1.3 aldehyde dehydrogenase (NAD+) oxidation - Homo sapiens - 1.2.1.3 aldehyde dehydrogenase (NAD+) oxidation - Mus musculus - 1.2.1.3 aldehyde dehydrogenase (NAD+) oxidation - Saccharomyces cerevisiae - 1.2.1.31 L-aminoadipate-semialdehyde dehydrogenase oxidation - Homo sapiens Q4L235 1.2.1.32 aminomuconate-semialdehyde dehydrogenase oxidation - Bordetella sp. - 1.2.1.36 retinal dehydrogenase oxidation - Mus musculus Q9JHW9, Q62148, P24549, Q62148, P24549, Q9JHW9 1.2.1.36 retinal dehydrogenase oxidation - Rattus norvegicus P51647, P51647, Q63639, Q63639, Q8K4D8, Q8K4D8 1.2.1.39 phenylacetaldehyde dehydrogenase oxidation - Pseudomonas putida B1N7H3 1.2.1.4 aldehyde dehydrogenase (NADP+) oxidation - Homo sapiens - 1.2.1.4 aldehyde dehydrogenase (NADP+) oxidation - Mammalia - 1.2.1.4 aldehyde dehydrogenase (NADP+) oxidation - Mus musculus Q540D7 1.2.1.4 aldehyde dehydrogenase (NADP+) oxidation - Oryctolagus cuniculus - 1.2.1.41 glutamate-5-semialdehyde dehydrogenase oxidation - Cedrela odorata B1P5P4 1.2.1.41 glutamate-5-semialdehyde dehydrogenase oxidation - Ceiba pentandra B1P5P5, B1P5P6 1.2.1.41 glutamate-5-semialdehyde dehydrogenase oxidation - Oryza sativa Q941T1 1.2.1.41 glutamate-5-semialdehyde dehydrogenase oxidation - Pachira quinata B1P5P3 1.2.1.41 glutamate-5-semialdehyde dehydrogenase oxidation - Schizolobium parahyba B1P5P7, B1P5P8 1.2.1.41 glutamate-5-semialdehyde dehydrogenase oxidation - Thermus thermophilus - 1.2.1.44 cinnamoyl-CoA reductase oxidation - Arabidopsis thaliana - 1.2.1.44 cinnamoyl-CoA reductase oxidation - Oryza sativa - 1.2.1.44 cinnamoyl-CoA reductase oxidation - Populus tremuloides Q9M631 1.2.1.44 cinnamoyl-CoA reductase oxidation - Solanum lycopersicum Q4U1I4, Q4U1I5 1.2.1.44 cinnamoyl-CoA reductase oxidation - Triticum aestivum Q4KUK8 1.2.1.46 formaldehyde dehydrogenase oxidation - Homo sapiens - 1.2.1.5 aldehyde dehydrogenase [NAD(P)+] oxidation - Oryza sativa Q0DZ46, Q53NG8, Q69P84, Q6H627, Q7XR89, Q9FRX7, Q9LRE9, Q9LRI6 1.2.1.5 aldehyde dehydrogenase [NAD(P)+] oxidation - Sphingopyxis macrogoltabida - 1.2.1.65 salicylaldehyde dehydrogenase oxidation - Stenotrophomonas sp. RMSK - 1.2.1.7 benzaldehyde dehydrogenase (NADP+) oxidation - Acinetobacter baylyi - 1.2.1.71 succinylglutamate-semialdehyde dehydrogenase oxidation - Escherichia coli - 1.2.1.72 erythrose-4-phosphate dehydrogenase oxidation - Escherichia coli - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Atriplex hortensis - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Avena sativa - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Beta vulgaris - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Embryophyta - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Hordeum vulgare - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Jatropha curcas B2BBY6 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Leymus chinensis - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Oryza sativa O24174, Q84LK3, O24174, Q84LK3, B3VMC0, B3VMC1, B3VMC2 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Pisum sativum - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Pseudomonas aeruginosa Q9HTJ1, Q9HTJ1, Q9HTJ1 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Suaeda liaotungensis - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Suaeda salsa Q155V4 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Sus scrofa - 1.2.1.8 betaine-aldehyde dehydrogenase oxidation - Zoysia tenuifolia Q6BD86, Q6BD88, Q6BD90, Q6BD91, Q6BD93, Q6BD95, Q6BD99, Q6BDA3, Q6BDA4 1.2.1.88 L-glutamate gamma-semialdehyde dehydrogenase oxidation - Oryza sativa Q0DHN6 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Arabidopsis thaliana - 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Bacillus cereus Q2HQS1 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Bacillus licheniformis Q2HQS0 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Bacillus sp. (in: Bacteria) - 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Bacillus thuringiensis Q2HQR5 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Chlamydomonas reinhardtii - 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Clostridioides difficile Q2HQR4 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Clostridium acetobutylicum Q2HQR9 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Clostridium pasteurianum Q2HQR7 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Clostridium perfringens Q2HQR8 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Clostridium sporogenes Q2HQR6 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Oryza sativa Q6Z9G0 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Spinacia oleracea - 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Streptococcus agalactiae Q2HQS4 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Streptococcus equinus Q3C1A6, Q3C1A6 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Streptococcus mutans Q59931 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Streptococcus pyogenes Q2HQR3 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Streptococcus sp. Q2HQS3 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Synechococcus elongatus PCC 7942 = FACHB-805 - 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Talipariti tiliaceum - 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Triticum aestivum - 1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+) oxidation - Zea mays - 1.2.1.B23 4,4'-diaponeurosporen-aldehyde dehydrogenase oxidation - Staphylococcus aureus A0A0H3KDU5 1.2.3.14 abscisic-aldehyde oxidase oxidation - Arabidopsis sp. - 1.2.3.14 abscisic-aldehyde oxidase oxidation - Solanum lycopersicum - 1.2.3.4 oxalate oxidase oxidation - Abortiporus biennis - 1.2.3.4 oxalate oxidase oxidation - Amaranthus spinosus - 1.2.3.4 oxalate oxidase oxidation - Hordeum vulgare - 1.2.3.4 oxalate oxidase oxidation - Triticum aestivum P15290 1.21.3.1 isopenicillin-N synthase oxidation - Aspergillus nidulans P05326 1.21.3.3 reticuline oxidase oxidation - Eschscholzia californica P30986 1.21.3.7 tetrahydrocannabinolic acid synthase oxidation oxidative cyclization Cannabis sativa - 1.3.1.20 trans-1,2-dihydrobenzene-1,2-diol dehydrogenase oxidation - Macaca fascicularis Q9TQS6 1.3.1.24 biliverdin reductase oxidation - Homo sapiens P53004 1.3.1.24 biliverdin reductase oxidation - Mus musculus - 1.3.1.24 biliverdin reductase oxidation - Rattus norvegicus - 1.3.1.33 protochlorophyllide reductase oxidation - Arabidopsis thaliana O48741, P21218, Q42536 1.3.1.33 protochlorophyllide reductase oxidation - Chroomonas mesostigmatica B0F840 1.3.1.33 protochlorophyllide reductase oxidation - Chroomonas pauciplastida B0F835 and B0F841 and B0F842 1.3.1.33 protochlorophyllide reductase oxidation - Gloeobacter violaceus - 1.3.1.33 protochlorophyllide reductase oxidation - Hemiselmis andersenii B0F833 and B0F836 and B0F837 1.3.1.33 protochlorophyllide reductase oxidation - Hemiselmis tepida B0F838 and B0F839 1.3.1.33 protochlorophyllide reductase oxidation - Hordeum vulgare Q42850 1.3.1.33 protochlorophyllide reductase oxidation - Microchaete diplosiphon A9UGZ2, C6KHP5 and Q6H056 and Q6H058 1.3.1.33 protochlorophyllide reductase oxidation - Pisum sativum Q01289 1.3.1.33 protochlorophyllide reductase oxidation - Synechocystis sp. - 1.3.1.33 protochlorophyllide reductase oxidation - Synechocystis sp. PCC 6803 - 1.3.1.33 protochlorophyllide reductase oxidation - Thermosynechococcus vestitus - 1.3.1.5 cucurbitacin DELTA23-reductase oxidation - Cucurbita maxima - 1.3.1.54 precorrin-6A reductase oxidation - Methanococcus maripaludis Q977V1 1.3.1.73 1,2-dihydrovomilenine reductase oxidation - Rauvolfia serpentina - 1.3.1.77 anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming] oxidation - Camellia sinensis Q6DV46 1.3.1.77 anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming] oxidation - Medicago truncatula Q84XT1 1.3.1.9 enoyl-[acyl-carrier-protein] reductase (NADH) oxidation - Escherichia coli P0AEK4, P0AEK4 1.3.1.9 enoyl-[acyl-carrier-protein] reductase (NADH) oxidation - Mycobacterium tuberculosis P9WGR1 1.3.1.9 enoyl-[acyl-carrier-protein] reductase (NADH) oxidation - Plasmodium falciparum - 1.3.1.9 enoyl-[acyl-carrier-protein] reductase (NADH) oxidation - Staphylococcus aureus - 1.3.1.9 enoyl-[acyl-carrier-protein] reductase (NADH) oxidation - Streptococcus pneumoniae Q8DR17 1.3.2.3 L-galactonolactone dehydrogenase oxidation - Arabidopsis thaliana Q9SU56 1.3.3.11 pyrroloquinoline-quinone synthase oxidation - Deinococcus radiodurans - 1.3.3.11 pyrroloquinoline-quinone synthase oxidation - Escherichia coli - 1.3.3.11 pyrroloquinoline-quinone synthase oxidation - Klebsiella pneumoniae P27505, P27505, P27505 1.3.3.11 pyrroloquinoline-quinone synthase oxidation - Methylorubrum extorquens Q49150 1.3.3.5 bilirubin oxidase oxidation - Albifimbria verrucaria - 1.3.3.6 acyl-CoA oxidase oxidation - Rattus norvegicus - 1.3.7.8 benzoyl-CoA reductase oxidation - Geobacter metallireducens - 1.3.7.8 benzoyl-CoA reductase oxidation - Thauera aromatica - 1.3.8.7 medium-chain acyl-CoA dehydrogenase oxidation - Rattus norvegicus - 1.3.8.8 long-chain acyl-CoA dehydrogenase oxidation - Homo sapiens - 1.3.8.8 long-chain acyl-CoA dehydrogenase oxidation - Mus musculus - 1.3.98.3 coproporphyrinogen dehydrogenase oxidation - Escherichia coli - 1.3.99.23 all-trans-retinol 13,14-reductase oxidation - Homo sapiens - 1.3.99.23 all-trans-retinol 13,14-reductase oxidation - Mus musculus - 1.4.1.21 aspartate dehydrogenase oxidation - Thermotoga maritima Q9X1X6 1.4.3.19 glycine oxidase oxidation - Bacillus subtilis - 1.4.3.22 diamine oxidase oxidation - Cucumis sativus - 1.5.1.2 pyrroline-5-carboxylate reductase oxidation - Homo sapiens P32322 1.5.1.2 pyrroline-5-carboxylate reductase oxidation - Mycobacterium tuberculosis - 1.5.1.2 pyrroline-5-carboxylate reductase oxidation - Neisseria meningitidis - 1.5.1.2 pyrroline-5-carboxylate reductase oxidation - Streptococcus pyogenes - 1.5.1.32 vomilenine reductase oxidation - Rauvolfia serpentina - 1.5.1.5 methylenetetrahydrofolate dehydrogenase (NADP+) oxidation - Homo sapiens - 1.5.1.5 methylenetetrahydrofolate dehydrogenase (NADP+) oxidation - Leishmania major - 1.5.1.5 methylenetetrahydrofolate dehydrogenase (NADP+) oxidation - Saccharomyces cerevisiae - 1.5.1.6 formyltetrahydrofolate dehydrogenase oxidation - Rattus norvegicus - 1.6.5.2 NAD(P)H dehydrogenase (quinone) oxidation - Cavia porcellus Q8CHK7 1.6.5.2 NAD(P)H dehydrogenase (quinone) oxidation - Mus musculus Q64669 1.6.5.2 NAD(P)H dehydrogenase (quinone) oxidation - Rattus norvegicus P05982 1.6.5.2 NAD(P)H dehydrogenase (quinone) oxidation - Saccharomyces cerevisiae Q07923 1.7.1.6 azobenzene reductase oxidation - Bacillus amyloliquefaciens B3VPZ9 1.7.1.6 azobenzene reductase oxidation - Bacillus sp. (in: Bacteria) Q9FAW5 1.7.1.6 azobenzene reductase oxidation - Bacillus sp. B29 C0STY0, C0STY1 1.7.1.6 azobenzene reductase oxidation - Bacillus subtilis O07529 1.7.1.6 azobenzene reductase oxidation - Brevibacillus laterosporus - 1.7.1.6 azobenzene reductase oxidation - Cereibacter sphaeroides Q8GKS3, Q8GKS3, Q8GKS3 1.7.1.6 azobenzene reductase oxidation - Enterococcus faecalis Q831B2, Q831B2 1.7.1.6 azobenzene reductase oxidation - Enterococcus faecium D0EFL2 1.7.1.6 azobenzene reductase oxidation - Escherichia coli Q8X9S9, P41407, P41407 1.7.1.6 azobenzene reductase oxidation - Geobacillus stearothermophilus Q8RR37 1.7.1.6 azobenzene reductase oxidation - Pigmentiphaga kullae Q6YAN1 1.7.1.6 azobenzene reductase oxidation - Staphylococcus aureus Q50H63 1.7.1.6 azobenzene reductase oxidation - Xenophilus azovorans Q8KU07 1.7.1.B4 azobenzene reductase [NADH] oxidation - Bacillus badius - 1.7.3.3 factor-independent urate hydroxylase oxidation - Arthrobacter globiformis D0VWQ1 1.7.3.3 factor-independent urate hydroxylase oxidation - Aspergillus flavus Q00511 1.7.3.3 factor-independent urate hydroxylase oxidation - Cyberlindnera jadinii - 1.7.3.3 factor-independent urate hydroxylase oxidation - Geobacillus thermocatenulatus DQ887577 1.7.3.3 factor-independent urate hydroxylase oxidation - Saccharomyces cerevisiae - 1.8.1.2 assimilatory sulfite reductase (NADPH) oxidation - Acidithiobacillus ferrooxidans - 1.8.1.2 assimilatory sulfite reductase (NADPH) oxidation - Saccharomyces cerevisiae - 1.8.1.4 dihydrolipoyl dehydrogenase oxidation - Homo sapiens P09622 1.8.1.4 dihydrolipoyl dehydrogenase oxidation catalyzes reoxidation of reduced lipoate attached to H-protein, a lipoic acid-containing protein Pisum sativum - 1.8.1.8 protein-disulfide reductase oxidation - Pyrococcus furiosus - 1.8.2.2 thiosulfate dehydrogenase oxidation - Allochromatium vinosum - 1.8.2.2 thiosulfate dehydrogenase oxidation - halophilic bacterium - 1.8.2.4 dimethyl sulfide:cytochrome c2 reductase oxidation - Rhodovulum sulfidophilum Q8GPG1, Q8GPG3, Q8GPG4 1.8.5.4 bacterial sulfide:quinone reductase oxidation - Acidithiobacillus ferrooxidans - 1.8.5.4 bacterial sulfide:quinone reductase oxidation - Allochromatium vinosum - 1.8.5.4 bacterial sulfide:quinone reductase oxidation - Aquifex aeolicus - 1.8.5.4 bacterial sulfide:quinone reductase oxidation - Rhodobacter capsulatus - 1.8.7.1 assimilatory sulfite reductase (ferredoxin) oxidation - Cyanidioschyzon merolae - 1.8.98.2 sulfiredoxin oxidation - Homo sapiens - 1.8.98.2 sulfiredoxin oxidation - Mus musculus - 1.8.98.2 sulfiredoxin oxidation - Saccharomyces cerevisiae - 1.8.99.2 adenylyl-sulfate reductase oxidation - Arabidopsis thaliana - 1.8.99.2 adenylyl-sulfate reductase oxidation - Bacillus subtilis - 1.8.99.2 adenylyl-sulfate reductase oxidation - Pseudomonas aeruginosa - 1.97.1.1 chlorate reductase oxidation - Alicycliphilus denitrificans - 1.97.1.1 chlorate reductase oxidation - Dechloromonas hortensis - 1.97.1.1 chlorate reductase oxidation - Dechlorosoma sp. - 1.97.1.1 chlorate reductase oxidation - Ideonella dechloratans - 1.97.1.1 chlorate reductase oxidation - Stutzerimonas chloritidismutans - 4.2.3.17 taxadiene synthase oxidation - Taxus cuspidata - 4.2.3.4 3-dehydroquinate synthase oxidation alcohol oxidation Xanthomonas oryzae - 7.1.1.9 cytochrome-c oxidase oxidation - eukaryota - 7.1.1.9 cytochrome-c oxidase oxidation - Homo sapiens - 7.1.1.9 cytochrome-c oxidase oxidation - Metapenaeus affinis Q85A99 7.1.1.9 cytochrome-c oxidase oxidation - Metapenaeus ensis Q71SU4 7.1.1.9 cytochrome-c oxidase oxidation - Metapenaeus sp. - 7.1.1.9 cytochrome-c oxidase oxidation - Mus musculus - 7.1.1.9 cytochrome-c oxidase oxidation - Mytilus edulis B0F2H7 7.1.1.9 cytochrome-c oxidase oxidation - Panulirus japonicus - 7.1.1.9 cytochrome-c oxidase oxidation - Parapenaeus fissuroides Q85JA8 7.1.1.9 cytochrome-c oxidase oxidation - Parapenaeus longirostris - 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus aztecus Q71SU0 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus brasiliensis O78772 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus brevirostris - 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus californiensis Q8HJI1 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus chinensis Q0PRL0 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus indicus Q71ST7 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus japonicus - 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus latisulcatus Q71SS9 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus merguiensis Q85PT3 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus monodon - 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus notialis Q9XMI0 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus semisulcatus Q71SU3 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus setiferus - 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus stylirostris Q8HJI7 7.1.1.9 cytochrome-c oxidase oxidation - Penaeus vannamei - 7.1.1.9 cytochrome-c oxidase oxidation - Pleoticus muelleri - 7.1.1.9 cytochrome-c oxidase oxidation - Pseudomonas putida Q88RM6 7.1.1.9 cytochrome-c oxidase oxidation - Rattus norvegicus - 7.1.1.9 cytochrome-c oxidase oxidation - Solenocera agassizii - 7.1.1.9 cytochrome-c oxidase oxidation - Solenocera crassicornis Q85JA4 7.1.1.9 cytochrome-c oxidase oxidation - Solenocera koelbeli O99896 7.1.1.9 cytochrome-c oxidase oxidation - Synechocystis sp. -