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CAZyme Information: SMAC_09130-t26_1-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 | Sordaria macrospora | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Sordariomycetes; ; Sordariaceae; Sordaria; Sordaria macrospora | |||||||||||
| CAZyme ID | SMAC_09130-t26_1-p1 | |||||||||||
| CAZy Family | GT20 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| 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 | 68 | 334 | 1.6e-66 | 0.537117903930131 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 396238 | FAD_binding_4 | 7.66e-26 | 70 | 208 | 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. |
| 223354 | GlcD | 8.30e-25 | 69 | 349 | 31 | 315 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
| 273751 | FAD_lactone_ox | 0.009 | 75 | 141 | 20 | 86 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 1.17e-27 | 28 | 239 | 37 | 236 | |
| 1.28e-26 | 47 | 239 | 40 | 225 | |
| 8.48e-26 | 28 | 275 | 26 | 264 | |
| 8.48e-26 | 28 | 275 | 26 | 264 | |
| 1.56e-25 | 28 | 275 | 26 | 264 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.54e-27 | 28 | 309 | 1 | 274 | Structure of berberine bridge enzyme in complex with (S)-scoulerine [Eschscholzia californica] |
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| 1.85e-27 | 28 | 309 | 7 | 280 | Structure of berberine bridge enzyme in complex with dehydroscoulerine [Eschscholzia californica] |
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| 2.10e-27 | 28 | 309 | 26 | 299 | Structure of berberine bridge enzyme in complex with (S)-reticuline [Eschscholzia californica],3D2H_A Structure of berberine bridge enzyme from Eschscholzia californica, monoclinic crystal form [Eschscholzia californica],3D2J_A Structure of berberine bridge enzyme from Eschscholzia californica, tetragonal crystal form [Eschscholzia californica] |
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| 2.51e-27 | 28 | 309 | 7 | 280 | Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline [Eschscholzia californica] |
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| 1.28e-26 | 28 | 309 | 26 | 299 | Berberine bridge enzyme G164A variant, a reticuline dehydrogenase [Eschscholzia californica],4PZF_B Berberine bridge enzyme G164A variant, a reticuline dehydrogenase [Eschscholzia californica],4PZF_C Berberine bridge enzyme G164A variant, a reticuline dehydrogenase [Eschscholzia californica],4PZF_D Berberine bridge enzyme G164A variant, a reticuline dehydrogenase [Eschscholzia californica] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.08e-26 | 28 | 309 | 26 | 299 | Reticuline oxidase OS=Eschscholzia californica OX=3467 GN=BBE1 PE=1 SV=1 |
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| 4.51e-24 | 28 | 276 | 3 | 231 | FAD-linked oxidoreductase pyvE OS=Aspergillus violaceofuscus (strain CBS 115571) OX=1450538 GN=pyvE PE=3 SV=1 |
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| 3.84e-23 | 70 | 239 | 61 | 224 | Xylooligosaccharide oxidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=xylO PE=1 SV=1 |
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| 4.68e-23 | 68 | 333 | 73 | 322 | Reticuline oxidase OS=Papaver somniferum OX=3469 GN=BBE1 PE=2 SV=1 |
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| 1.42e-22 | 70 | 283 | 64 | 281 | FAD-linked oxidoreductase pytB OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pytB PE=2 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000029 | 0.000004 |