sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
7-432
0e+00
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
The actual alignment was detected with superfamily member TIGR01678:
Pssm-ID: 273751 [Multi-domain] Cd Length: 438 Bit Score: 701.27 E-value: 0e+00
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
7-432
0e+00
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
Pssm-ID: 273751 [Multi-domain] Cd Length: 438 Bit Score: 701.27 E-value: 0e+00
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC: ...
180-438
5.80e-123
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.
Pssm-ID: 427663 [Multi-domain] Cd Length: 258 Bit Score: 357.73 E-value: 5.80e-123
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
7-432
0e+00
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
Pssm-ID: 273751 [Multi-domain] Cd Length: 438 Bit Score: 701.27 E-value: 0e+00
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC: ...
180-438
5.80e-123
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.
Pssm-ID: 427663 [Multi-domain] Cd Length: 258 Bit Score: 357.73 E-value: 5.80e-123
FAD-linked oxidoreductase; This model represents a family of bacterial oxidoreductases with ...
10-439
5.62e-88
FAD-linked oxidoreductase; This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae.
Pssm-ID: 130740 [Multi-domain] Cd Length: 419 Bit Score: 274.07 E-value: 5.62e-88
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ...
12-439
1.04e-47
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3). This enzyme catalyzes the final step in ascorbic acid biosynthesis in higher plants. This protein is homologous to ascorbic acid biosynthesis enzymes of other species: L-gulono-gamma-lactone oxidase in rat and L-galactono-gamma-lactone oxidase in yeast. All three covalently bind the cofactor FAD.
Pssm-ID: 130737 [Multi-domain] Cd Length: 541 Bit Score: 171.40 E-value: 1.04e-47
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
21-156
6.88e-41
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
Pssm-ID: 426326 [Multi-domain] Cd Length: 139 Bit Score: 142.34 E-value: 6.88e-41
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
27-430
2.82e-36
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.
Pssm-ID: 273750 [Multi-domain] Cd Length: 557 Bit Score: 140.00 E-value: 2.82e-36
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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