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CATH Superfamily 3.40.605.10

Aldehyde Dehydrogenase; Chain A, domain 1

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Aldehyde Dehydrogenase; Chain A, domain 1
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 54 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Glutamate-5-semialdehyde dehydrogenase. [EC: 1.2.1.41]
L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH.
    		 1062 A0A009HBM5 A0A009K3C2 A0A009PV92 A0A009SH94 A0A009SQ34 A0A015Q5E5 A0A015ZXD1 A0A016CQE0 A0A016I645 A0A026V361
    (1052 more...)
    Betaine-aldehyde dehydrogenase. [EC: 1.2.1.8]
    Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH.
    • In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine.
    • This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria.
    • In contrast, different enzymes are involved in the first reaction.
    • In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17.
    • In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157.
    		 335 A0A009GR72 A0A009KCL7 A0A009QQP7 A0A009SL83 A0A009SWP2 A0A062DPQ6 A0A062FBQ0 A0A062FVR1 A0A069BG34 A0A070F9D7
    (325 more...)
    Succinylglutamate-semialdehyde dehydrogenase. [EC: 1.2.1.71]
    N-succinyl-L-glutamate 5-semialdehyde + NAD(+) + H(2)O = N-succinyl-L- glutamate + NADH.
    • This is the fourth enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine.
    • This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA.
    • The five enzymes involved in this pathway are EC 2.3.1.109, EC 3.5.3.23, EC 2.6.1.11, EC 1.2.1.71 and EC 3.5.1.96.
    		 304 A0A026UED9 A0A028AK67 A0A028EBM5 A0A029HZS7 A0A029ITZ3 A0A066Q7E3 A0A070ETG6 A0A070T441 A0A074I2I8 A0A078LHS4
    (294 more...)
    L-glutamate gamma-semialdehyde dehydrogenase. [EC: 1.2.1.88]
    L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH.
    • This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway.
    • (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde.
    • In many bacterial species, both activities are carried out by a single bifunctional enzyme.
    • The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate.
    • NADP(+) can also act as acceptor, but with lower activity.
    • Formerly EC 1.5.1.12.
    		 218 A0A023P0I1 A0A024RAD8 A0A063XE08 A0A069XGW6 A0A070SYJ5 A0A094WGV7 A0A0B5NF19 A0A0D6GKM3 A0A0E1APW1 A0A0E1LVT6
    (208 more...)
    Aldehyde dehydrogenase (NAD(+)). [EC: 1.2.1.3]
    An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH.
    • Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
    • Formerly EC 1.1.1.70.
    		 196 A0A045HU59 A0A0D6GJB8 A0A0E1AHD6 A0A0E1AKH2 A0A0E1VMG5 A0A0E1VP50 A0A0E1X8G8 A0A0E1XCL6 A0A0G7HP87 A0A0H3K677
    (186 more...)
    Methylmalonate-semialdehyde dehydrogenase (CoA acylating). [EC: 1.2.1.27]
    2-methyl-3-oxopropanoate + CoA + H(2)O + NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH.
    • Also converts 3-oxopropanoate into acetyl-CoA.
    • The reaction occurs in two steps with the decarboxylation process preceding CoA-binding.
    • Bicarbonate rather than CO(2) is released as a final product.
    		 176 A0A024R6G4 A0A063XH35 A0A080VFN0 A0A0A0WQ73 A0A0B6BM87 A0A0D0QLM9 A0A0D0R4D4 A0A0D1R7U2 A0A0E0TAQ3 A0A0E0UTY1
    (166 more...)
    Alcohol dehydrogenase. [EC: 1.1.1.1]
    (1) A primary alcohol + NAD(+) = an aldehyde + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.
    • Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol.
    • The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
    		 127 A0A023YWD7 A0A025CD77 A0A026V8A2 A0A028A9Z9 A0A028E6I5 A0A069XKQ8 A0A070UZF6 A0A073FYU1 A0A073HWC3 A0A073UK46
    (117 more...)
    Acetaldehyde dehydrogenase (acetylating). [EC: 1.2.1.10]
    Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH.
    • Also acts, more slowly, on glycolaldehyde, propanal and butanal.
    • In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39.
    • The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87.
    • Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols.
    • NADP(+) can replace NAD(+) but the rate of reaction is much slower.
    		 124 A0A023YWD7 A0A025CD77 A0A026V8A2 A0A028A9Z9 A0A028E6I5 A0A069XKQ8 A0A070UZF6 A0A073FYU1 A0A073HWC3 A0A073UK46
    (114 more...)
    Aminobutyraldehyde dehydrogenase. [EC: 1.2.1.19]
    4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH.
    • The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates.
    • The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54).
    • As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate.
    • Formerly EC 1.5.1.35.
    		 106 A0A027ZLX2 A0A028E005 A0A029I382 A0A029IVP3 A0A037Y594 A0A069XEG3 A0A090NBN8 A0A0A0FBZ3 A0A0A8U7E1 A0A0C2E7E4
    (96 more...)
    Succinate-semialdehyde dehydrogenase (NADP(+)). [EC: 1.2.1.79]
    Succinate semialdehyde + NADP(+) + H(2)O = succinate + NADPH.
    • This enzyme participates in the degradation of glutamate and 4-aminobutyrate.
    • It is similar to EC 1.2.1.24 and EC 1.2.1.16 but is specific for NADP(+).
    • The enzyme from Escherichia coli is 20-fold more active with NADP(+) than NAD(+).
    		 59 A0A045JTD4 A0A049DLQ0 A0A070STD3 A0A094Y301 A0A0E1M285 A0A0E2W6E6 A0A0E8WS10 A0A0H3L4Y9 A0A0H3LGA9 A0A0H3MSE4
    (49 more...)
    Phenylacetaldehyde dehydrogenase. [EC: 1.2.1.39]
    Phenylacetaldehyde + NAD(+) + H(2)O = phenylacetate + NADH.
      		 52 A0A024L396 A0A027ZPW4 A0A028E166 A0A070FI73 A0A070SIL6 A0A070UY69 A0A073FYN8 A0A074INC4 A0A080G6J2 A0A0A0FC35
      (42 more...)
      Aldehyde dehydrogenase (NAD(P)(+)). [EC: 1.2.1.5]
      An aldehyde + NAD(P)(+) + H(2)O = a carboxylate + NAD(P)H.
        		 52 A0A024R5D8 A0A037YAA6 A0A069XLJ5 A0A0E0TXD9 A0A0E1LYL3 A0A0E1SRQ9 A0A0L8VGX9 A0A0L8VRP0 A0A0M7NQY8 A0A140NAG2
        (42 more...)
        Succinate-semialdehyde dehydrogenase (NAD(P)(+)). [EC: 1.2.1.16]
        Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H.
          		 41 A0A024L3N1 A0A069XL49 A0A070SNM2 A0A0E1LX54 A0A0E8WS10 A0A0H3L4Y9 A0A0K2HS90 A0A0L8VVD7 A0A0M7NV91 A0A109SK26
          (31 more...)
          Proline dehydrogenase. [EC: 1.5.5.2]
          L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol.
          • The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor.
          • In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88.
          • Both activities are carried out by the same enzyme in enterobacteria.
          • Formerly EC 1.5.99.8.
          		 25 A0A069XGW6 A0A070SYJ5 A0A094WGV7 A0A0D6GKM3 A0A0E1LVT6 A0A0F7J5N8 A0A0H3NAG7 A0A0M9JAG6 A0A0U1FEH9 A0A0W4MGL3
          (15 more...)
          Retinal dehydrogenase. [EC: 1.2.1.36]
          Retinal + NAD(+) + H(2)O = retinoate + NADH.
          • Acts on both the 11-trans- and 13-cis-forms of retinal.
          		 24 A0A024RC95 A0A1U7QDB4 A0A226PKF6 G2HJM2 O93344 O94788 P00352 P15437 P24549 P27463
          (14 more...)
          3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase. [EC: 1.2.1.91]
          3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP(+) + H(2)O = 3-oxo-5,6- dehydrosuberyl-CoA + NADPH.
          • The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyzes EC 3.3.2.12.
          • Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway.
          • Formerly EC 1.17.1.7.
          		 21 A0A070VA51 A0A0A0F843 A0A0E1LWY3 A0A0E1SSD9 A0A1X3IQ56 A0A236R591 A0A236SJA7 A0A3R0DLC4 D7XYZ4 E3PLB8
          (11 more...)
          Oxepin-CoA hydrolase. [EC: 3.3.2.12]
          2-oxepin-2(3H)-ylideneacetyl-CoA + H(2)O = 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde.
          • The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyzes EC 1.17.1.7.
          • Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway.
          • The enzyme from Escherichia coli also exhibits enoyl-CoA hydratase activity utilizing crotonyl-CoA as a substrate.
          • Formerly EC 3.7.1.16.
          		 21 A0A070VA51 A0A0A0F843 A0A0E1LWY3 A0A0E1SSD9 A0A1X3IQ56 A0A236R591 A0A236SJA7 A0A3R0DLC4 D7XYZ4 E3PLB8
          (11 more...)
          Glutamate 5-kinase. [EC: 2.7.2.11]
          ATP + L-glutamate = ADP + L-glutamate 5-phosphate.
          • The product rapidly cyclizes to 5-oxoproline and phosphate.
          		 19 A0A178VF78 A0A178VY37 A0A2J8Y5L2 A0A2R6RWV5 A0A2R9C489 B8AC46 K7D0Y1 O04015 O04226 O65361
          (9 more...)
          Succinate-semialdehyde dehydrogenase (NAD(+)). [EC: 1.2.1.24]
          Succinate semialdehyde + NAD(+) + H(2)O = succinate + NADH.
          • This enzyme participates in the degradation of glutamate and 4-aminobutyrate.
          • It is similar to EC 1.2.1.79 and EC 1.2.1.16 but is specific for NAD(+).
          		 18 A0A0B2BDQ2 A0A0E0NAJ8 A0A1E3FT19 A0A2D7VBK7 B2RS41 B9F3B6 P51649 P51650 Q1JUP4 Q3MSM3
          (8 more...)
          2,5-dioxovalerate dehydrogenase. [EC: 1.2.1.26]
          2,5-dioxopentanoate + NADP(+) + H(2)O = 2-oxoglutarate + NADPH.
            		 18 A0A0B2B3F9 A0A0B2BDM1 A0A0B2BDQ2 A0A0E3JWV7 A0A164W5L2 A0A1D8FUL9 A0A1E3FHF3 A0A1E3FT19 A0A1E3FVA0 A0A2D7VEJ0
            (8 more...)
            Lactaldehyde dehydrogenase. [EC: 1.2.1.22]
            (S)-lactaldehyde + NAD(+) + H(2)O = (S)-lactate + NADH.
              		 15 A0A024L3U1 A0A069XL70 A0A0E1LYT9 A0A1X3JHV9 A0A3R0DJR7 A4FW36 A6UQD0 A6UVT6 A6VH72 G0FF83
              (5 more...)
              Malonate-semialdehyde dehydrogenase (acetylating). [EC: 1.2.1.18]
              3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA + CO(2) + NAD(P)H.
                		 15 A0A024R6G4 A0A182HSV9 A0A182LEZ0 A0A182TG60 A0A182VA95 P52713 Q02252 Q02253 Q07536 Q17M80
                (5 more...)
                Glyceraldehyde-3-phosphate dehydrogenase (NADP(+)). [EC: 1.2.1.9]
                D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O = 3-phospho-D-glycerate + NADPH.
                  		 13 A0A091BRP1 A0A1H8ZRA0 A0A384L3A7 B9DHD2 P81406 P93338 Q1WIQ6 Q3C1A6 Q43272 Q59931
                  (3 more...)
                  Salicylaldehyde dehydrogenase. [EC: 1.2.1.65]
                  Salicylaldehyde + NAD(+) + H(2)O = salicylate + NADH.
                  • Involved in the naphthalene degradation pathway in some bacteria.
                  		 11 A0A010SI37 A0A1H4ID85 A0A1V4LNR9 A0A1Y0BCE6 P0A390 P0A391 Q05K17 Q05K27 Q6XUJ4 Q79P83
                  (1 more...)
                  Aldehyde dehydrogenase (NADP(+)). [EC: 1.2.1.4]
                  An aldehyde + NADP(+) + H(2)O = a carboxylate + NADPH.
                    		 11 A0A0L8VFR9 A6ZWI7 C7GTZ5 C8ZIW9 E9P9H2 G2WPB8 H0GPP5 N1NX93 P54115 Q56694
                    (1 more...)
                    Coniferyl-aldehyde dehydrogenase. [EC: 1.2.1.68]
                    Coniferyl aldehyde + H(2)O + NAD(P)(+) = ferulate + NAD(P)H.
                    • Also oxidizes other aromatic aldehydes, but not aliphatic aldehydes.
                    		 10 A0A0C7ATV9 A0A0H3C9G0 A0A1F0IW89 A0A1G5L9C4 A0A1S1BXL7 A0A2V2U1T5 A0A448BWK0 O86447 Q9A777 Q9I6C8
                    2-hydroxymuconate-6-semialdehyde dehydrogenase. [EC: 1.2.1.85]
                    2-hydroxymuconate-6-semialdehyde + NAD(+) + H(2)O = (2Z,4E)-2- hydroxyhexa-2,4-dienedioate + NADH.
                    • This substrate for this enzyme is formed by meta ring cleavage of catechol (EC 1.13.11.2), and is an intermediate in the bacterial degradation of several aromatic compounds.
                    • Has lower activity with benzaldehyde.
                    • Activity with NAD(+) is more than 10-fold higher than with NADP(+).
                    • Cf. EC 1.2.1.32.
                    		 9 A0A077KB55 A0A083UEJ3 A0A0B5KNB2 A0A1L7G4D7 A0A1V4LTV6 A0A368CZA0 P19059 P23105 Q7AXV2
                    Benzaldehyde dehydrogenase (NAD(+)). [EC: 1.2.1.28]
                    Benzaldehyde + NAD(+) + H(2)O = benzoate + NADH.
                      		 9 A0A0T8PXP7 A0A164UG36 A0A172WS83 A0A1B2B2X6 L8ACD9 O06478 P43503 Q7AXU2 Q84DC3
                      Glycolaldehyde dehydrogenase. [EC: 1.2.1.21]
                      Glycolaldehyde + NAD(+) + H(2)O = glycolate + NADH.
                        		 9 A0A024L3U1 A0A069XL70 A0A0E1LYT9 A0A1X3JHV9 A0A3R0DJR7 G0FF83 H4UIQ0 I2X4U3 P25553
                        Formyltetrahydrofolate dehydrogenase. [EC: 1.5.1.6]
                        10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + NADPH.
                          		 8 O75891 P28037 Q3SY69 Q5RFM9 Q63ZT8 Q6GNL7 Q8K009 Q8R0Y6
                          Vanillin dehydrogenase. [EC: 1.2.1.67]
                          Vanillin + NAD(+) + H(2)O = vanillate + NADH.
                            		 7 A0A0T8PXP7 A0A164UG36 A0A1B2B2X6 L8ACD9 O05619 O06478 O69763
                            Long-chain-fatty-acyl-CoA reductase. [EC: 1.2.1.50]
                            A long-chain aldehyde + CoA + NADP(+) = a long-chain acyl-CoA + NADPH.
                            • Together with EC 6.2.1.19 forms a fatty acid reductase system which produces the substrate of EC 1.14.14.3, thus being part of the bacterial luciferase system.
                            		 7 C7BN07 P08639 P12748 P23113 P29236 Q03324 Q7N577
                            4-trimethylammoniobutyraldehyde dehydrogenase. [EC: 1.2.1.47]
                            4-trimethylammoniobutanal + NAD(+) + H(2)O = 4-trimethylammoniobutanoate + NADH.
                              		 6 P49189 Q29228 Q2KJH9 Q5R8A4 Q9JLJ2 Q9JLJ3
                              Aminomuconate-semialdehyde dehydrogenase. [EC: 1.2.1.32]
                              2-aminomuconate 6-semialdehyde + NAD(+) + H(2)O = 2-aminomuconate + NADH.
                              • Also acts on 2-hydroxymuconate semialdehyde.
                              		 6 A9YD19 Q0P5F9 Q66I21 Q8BH00 Q9H2A2 Q9KWS5
                              Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)). [EC: 1.2.1.90]
                              D-glyceraldehyde 3-phosphate + NAD(P)(+) + H(2)O = 3-phospho-D-glycerate + NAD(P)H.
                              • The enzyme is part of the modified Embden-Meyerhof-Parnas pathway of the archaeon Thermoproteus tenax (cf. EC 1.2.1.9).
                              		 4 A0A0E3K5I1 D0KR08 O57693 Q97U30
                              L-aminoadipate-semialdehyde dehydrogenase. [EC: 1.2.1.31]
                              (S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H.
                              • (S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
                              		 4 P49419 Q2KJC9 Q64057 Q9DBF1
                              Beta-apo-4'-carotenal oxygenase. [EC: 1.2.1.82]
                              4'-apo-beta,psi-caroten-4'-al + NAD(+) + H(2)O = neurosporaxanthin + NADH.
                              • Neurosporaxanthin is responsible for the orange color of of Neurospora.
                              		 4 A0A0I9Z9H7 F6IBC7 Q1K615 Q870P2
                              Succinate-semialdehyde dehydrogenase (acetylating). [EC: 1.2.1.76]
                              Succinate semialdehyde + CoA + NADP(+) = succinyl-CoA + NADPH.
                              • Catalyzes the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde.
                              • The enzyme has been described in Clostridium kluyveri, where it participates in succinate fermentation, and in Metallosphaera sedula, where it participates in the 3-hydroxypropanoate/4-hydroxybutyrate cycle, an autotrophic CO(2) fixation pathway found in some thermoacidophilic archaea.
                              		 2 B9E5D9 P38947
                              D-glyceraldehyde dehydrogenase (NADP(+)). [EC: 1.2.1.89]
                              D-glyceraldehyde + NADP(+) + H(2)O = D-glycerate + NADPH.
                              • The enzyme from the archaea Thermoplasma acidophilum and Picrophilus torridus is involved in the non-phosphorylative Entner-Doudoroff pathway, cf. EC 1.2.99.8.
                              		 2 Q6L285 Q9HK01
                              4,4'-diapolycopenoate synthase. [EC: 1.2.99.10]
                              (1) 4,4'-diapolycopen-4-al + H(2)O + acceptor = 4,4'-diapolycopen-4-oate + reduced acceptor. (2) 4,4'-diapolycopene-4,4'-dial + 2 H(2)O + 2 acceptor = 4,4'-diapolycopene-4,4'-dioate + 2 reduced acceptor.
                              • The enzyme has been described from the bacteria Methylomonas sp. 16a and Bacillus indicus.
                              		 2 P0DPF0 Q4VKV0
                              Geranial dehydrogenase. [EC: 1.2.1.86]
                              Geranial + H(2)O + NAD(+) = geranate + NADH.
                              • Does not act on neral.
                              • Formerly EC 1.2.1.n3.
                              		 2 H1ZV37 W8X5L1
                              4-(hydroxymethyl)benzenesulfonate dehydrogenase. [EC: 1.1.1.257]
                              4-(hydroxymethyl)benzenesulfonate + NAD(+) = 4-formylbenzenesulfonate + NADH.
                              • Involved in the toluene-4-sulfonate degradation pathway in Comamonas testosteroni.
                              		 2 P94682 Q9AHG1
                              4-hydroxybenzaldehyde dehydrogenase (NADP(+)). [EC: 1.2.1.96]
                              4-hydroxybenzaldehyde + NADP(+) + H(2)O = 4-hydroxybenzoate + NADPH.
                              • Involved in the aerobic pathway for degradation of toluene, 4-methylphenol, and 2,4-xylenol by several Pseudomonas strains.
                              • The enzyme is also active with 4-hydroxy-3-methylbenzaldehyde.
                              • Cf. EC 1.2.1.64.
                              		 2 A0A077FA43 Q59702
                              3,6-anhydro-alpha-L-galactose dehydrogenase. [EC: 1.2.1.92]
                              3,6-anhydro-alpha-L-galactopyranose + NAD(P)(+) + H(2)O = 3,6-anhydro-L- galactonate + NAD(P)H.
                              • The enzyme, characterized from the marine bacterium Vibrio sp. EJY3, is involved in a degradation pathway for 3,6-anhydro-alpha-L- galactose, a major component of the polysaccharides produced by red macroalgae, such as agarose and porphyran.
                              		 1 H2IFE7
                              2-hydroxy-2-methylpropanal dehydrogenase. [EC: 1.2.1.98]
                              2-hydroxy-2-methylpropanal + NAD(+) + H(2)O = 2-hydroxyisobutanoate + NADH.
                              • This bacterial enzyme is involved in the degradation pathways of the alkene 2-methylpropene and the fuel oxygenate methyl tert-butyl ether (MTBE), a widely occurring groundwater contaminant.
                              		 1 Q3YAT5
                              2-formylbenzoate dehydrogenase. [EC: 1.2.1.78]
                              2-formylbenzoate + NAD(+) + H(2)O = phthalate + NADH.
                              • The enzyme is involved in phenanthrene degradation.
                              		 1 Q79EM7
                              Benzaldehyde dehydrogenase (NADP(+)). [EC: 1.2.1.7]
                              Benzaldehyde + NADP(+) + H(2)O = benzoate + NADPH.
                                		 1 Q84DC3
                                3-succinoylsemialdehyde-pyridine dehydrogenase. [EC: 1.2.1.83]
                                4-oxo-4-(pyridin-3-yl)butanal + NADP(+) + H(2)O = 4-oxo-4-(pyridin-3- yl)butanoate + NADPH.
                                • The enzyme has been characterized from the soil bacterium Pseudomonas sp. HZN6.
                                • It participates in the nicotine degradation pathway.
                                		 1 H8ZPX2
                                3-sulfolactaldehyde dehydrogenase. [EC: 1.2.1.97]
                                (2S)-3-sulfolactaldehyde + NAD(P)(+) + H(2)O = (2S)-3-sulfolactate + NAD(P)H.
                                • The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway.
                                • Also acts on succinate semialdehyde.
                                		 1 P0DOV9
                                Long-chain-aldehyde dehydrogenase. [EC: 1.2.1.48]
                                A long-chain aldehyde + NAD(+) + H(2)O = a long-chain acid anion + NADH.
                                • The best substrate is dodecylaldehyde.
                                		 1 Q9FDS1
                                3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP(+)). [EC: 1.2.1.77]
                                Cis-3,4-dehydroadipyl-CoA semialdehyde + NADP(+) + H(2)O = cis-3,4- dehydroadipyl-CoA + NADPH.
                                • This enzyme catalyzes a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.
                                • Formerly EC 1.2.1.n1.
                                		 1 Q84HH8
                                Sulfoacetaldehyde dehydrogenase (acylating). [EC: 1.2.1.81]
                                2-sulfoacetaldehyde + CoA + NADP(+) = sulfoacetyl-CoA + NADPH.
                                • The enzyme is involved in degradation of sulfoacetate.
                                • In this pathway the reaction is catalyzed in the reverse direction.
                                • The enzyme is specific for sulfoacetaldehyde and NADP(+).
                                		 1 Q0K845
                                Sulfoacetaldehyde dehydrogenase. [EC: 1.2.1.73]
                                2-sulfoacetaldehyde + H(2)O + NAD(+) = sulfoacetate + NADH.
                                • Part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth.
                                • At physiological concentrations, NAD(+) cannot be replaced by NADP(+).
                                • Specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.
                                		 1 Q2BN77
                                Fluoroacetaldehyde dehydrogenase. [EC: 1.2.1.69]
                                Fluoroacetaldehyde + NAD(+) + H(2)O = fluoroacetate + NADH.
                                • The enzyme from Streptomyces cattleya has a high affinity for fluoroacetate and glycolaldehyde but not for acetaldehyde.
                                		 1 F8JX40