Species | Lomentospora prolificans | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans | |||||||||||
CAZyme ID | jhhlp_007450-t41_1-p1 | |||||||||||
CAZy Family | GH7 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 38 | 566 | 9.8e-172 | 0.9865900383141762 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 5.79e-31 | 93 | 231 | 2 | 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 | 5.19e-30 | 54 | 557 | 1 | 455 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
397178 | FAD-oxidase_C | 5.10e-12 | 449 | 556 | 142 | 247 | FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. |
183043 | PRK11230 | 2.86e-09 | 41 | 276 | 14 | 232 | glycolate oxidase subunit GlcD; Provisional |
178402 | PLN02805 | 8.87e-07 | 50 | 269 | 97 | 302 | D-lactate dehydrogenase [cytochrome] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 6 | 570 | 9 | 571 | |
6.24e-156 | 39 | 571 | 35 | 570 | |
1.77e-155 | 39 | 570 | 35 | 569 | |
9.64e-154 | 37 | 574 | 30 | 568 | |
5.29e-153 | 38 | 565 | 30 | 559 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.18e-120 | 39 | 565 | 5 | 522 | Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXD_B Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXE_A Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXE_B Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXF_A Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXF_B Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXP_A Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1],5FXP_B Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1] |
|
2.54e-111 | 38 | 559 | 7 | 514 | p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVE_B p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVF_A p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida] |
|
2.61e-111 | 38 | 559 | 8 | 515 | Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DII_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_A Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida] |
|
6.40e-110 | 34 | 570 | 8 | 559 | STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum],1W1L_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum] |
|
1.79e-109 | 34 | 570 | 8 | 559 | Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1E0Y_B Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.34e-110 | 38 | 559 | 8 | 515 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
|
1.30e-108 | 34 | 570 | 8 | 559 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
|
4.17e-16 | 83 | 276 | 32 | 218 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
|
1.06e-14 | 50 | 295 | 34 | 270 | Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1 |
|
6.21e-12 | 49 | 273 | 2 | 213 | Uncharacterized FAD-linked oxidoreductase Rv2280 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2280 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000051 | 0.000010 |
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