Species | Coccidioides immitis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides immitis | |||||||||||
CAZyme ID | CIHG_00344-t26_1-p1 | |||||||||||
CAZy Family | AA2 | |||||||||||
CAZyme Description | D-arabinono-1,4-lactone oxidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 27 | 235 | 3.6e-30 | 0.4606986899563319 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
273751 | FAD_lactone_ox | 9.66e-144 | 28 | 472 | 7 | 436 | 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. |
397924 | ALO | 2.54e-108 | 195 | 478 | 1 | 258 | 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. |
223354 | GlcD | 5.02e-44 | 26 | 471 | 21 | 450 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
215258 | PLN02465 | 4.64e-35 | 28 | 475 | 89 | 565 | L-galactono-1,4-lactone dehydrogenase |
396238 | FAD_binding_4 | 2.85e-34 | 36 | 171 | 1 | 139 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.35e-09 | 36 | 232 | 59 | 267 | |
1.66e-09 | 12 | 198 | 107 | 300 | |
3.34e-09 | 36 | 194 | 62 | 223 | |
4.19e-09 | 35 | 201 | 212 | 381 | |
4.30e-09 | 35 | 218 | 48 | 239 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.60e-28 | 23 | 245 | 110 | 331 | Assembly intermediate of the plant mitochondrial complex I [Brassica oleracea] |
|
3.36e-15 | 28 | 255 | 13 | 238 | Alditol Oxidase from Streptomyces coelicolor A3(2): Native Enzyme [Streptomyces coelicolor A3(2)],2VFS_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Xylitol [Streptomyces coelicolor A3(2)],2VFT_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sorbitol [Streptomyces coelicolor A3(2)],2VFU_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Mannitol [Streptomyces coelicolor A3(2)],2VFV_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sulphite [Streptomyces coelicolor A3(2)] |
|
8.35e-11 | 36 | 232 | 37 | 245 | Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale] |
|
1.97e-10 | 36 | 196 | 48 | 212 | Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens] |
|
1.97e-10 | 36 | 196 | 48 | 212 | Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.67e-203 | 9 | 526 | 24 | 556 | Putative D-arabinono-1,4-lactone oxidase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=alo-1 PE=3 SV=1 |
|
1.66e-126 | 19 | 472 | 9 | 514 | D-arabinono-1,4-lactone oxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALO1 PE=3 SV=1 |
|
6.46e-109 | 16 | 472 | 10 | 543 | D-arabinono-1,4-lactone oxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALO1 PE=1 SV=1 |
|
5.38e-107 | 23 | 472 | 16 | 513 | D-arabinono-1,4-lactone oxidase OS=Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OX=284811 GN=ALO1 PE=3 SV=1 |
|
3.43e-106 | 28 | 475 | 19 | 516 | D-arabinono-1,4-lactone oxidase OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=ALO1 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000054 | 0.000000 |
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