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CAZyme Information: AN0836-T-p1
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Aspergillus nidulans | |||||||||||
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| Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans | |||||||||||
| CAZyme ID | AN0836-T-p1 | |||||||||||
| CAZy Family | AA3 | |||||||||||
| CAZyme Description | Ortholog(s) have D-arabinono-1,4-lactone oxidase activity | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| AA7 | 28 | 224 | 1.2e-26 | 0.4366812227074236 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 273751 | FAD_lactone_ox | 5.20e-134 | 29 | 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 | 3.11e-102 | 197 | 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 | 4.85e-37 | 27 | 471 | 21 | 450 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
| 215258 | PLN02465 | 3.11e-33 | 29 | 438 | 89 | 522 | L-galactono-1,4-lactone dehydrogenase |
| 396238 | FAD_binding_4 | 5.97e-33 | 37 | 173 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 6.90e-13 | 37 | 219 | 59 | 252 | |
| 3.87e-12 | 37 | 219 | 62 | 254 | |
| 8.75e-11 | 82 | 471 | 121 | 491 | |
| 4.41e-09 | 37 | 212 | 63 | 248 | |
| 9.76e-09 | 12 | 209 | 14 | 219 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2.03e-25 | 24 | 246 | 110 | 330 | Assembly intermediate of the plant mitochondrial complex I [Brassica oleracea] |
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| 2.49e-16 | 29 | 207 | 13 | 186 | 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)] |
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| 5.39e-14 | 37 | 219 | 37 | 230 | 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] |
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| 1.20e-07 | 20 | 200 | 26 | 214 | Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens] |
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| 1.20e-07 | 20 | 200 | 26 | 214 | Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.13e-190 | 3 | 523 | 13 | 548 | 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 |
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| 6.17e-119 | 24 | 472 | 13 | 514 | D-arabinono-1,4-lactone oxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALO1 PE=3 SV=1 |
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| 6.99e-103 | 21 | 484 | 14 | 556 | D-arabinono-1,4-lactone oxidase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=ALO1 PE=3 SV=2 |
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| 3.87e-102 | 25 | 472 | 17 | 543 | D-arabinono-1,4-lactone oxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALO1 PE=1 SV=1 |
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| 2.95e-101 | 24 | 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 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000077 | 0.000000 |