Species | Trichosporon asahii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Basidiomycota; Tremellomycetes; ; Trichosporonaceae; Trichosporon; Trichosporon asahii | |||||||||||
CAZyme ID | EJT50180.1 | |||||||||||
CAZy Family | GH71 | |||||||||||
CAZyme Description | FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:J4UFM5] | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
EC | 1.1.3.38:1 |
---|
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 4 | 542 | 2.9e-217 | 0.9961685823754789 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 1.36e-28 | 67 | 208 | 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 | 5.08e-23 | 65 | 530 | 31 | 455 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
178402 | PLN02805 | 2.04e-14 | 14 | 211 | 65 | 274 | D-lactate dehydrogenase [cytochrome] |
397178 | FAD-oxidase_C | 2.63e-06 | 440 | 529 | 148 | 247 | FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. |
183043 | PRK11230 | 4.32e-05 | 69 | 530 | 59 | 471 | glycolate oxidase subunit GlcD; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
6.99e-260 | 3 | 552 | 27 | 587 | |
2.83e-259 | 3 | 552 | 27 | 587 | |
7.09e-257 | 3 | 552 | 27 | 587 | |
2.34e-255 | 3 | 552 | 27 | 587 | |
5.70e-249 | 3 | 548 | 8 | 562 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.10e-233 | 3 | 544 | 8 | 560 | 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] |
|
1.17e-232 | 3 | 544 | 8 | 560 | Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
|
2.35e-232 | 3 | 544 | 8 | 560 | STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum],1W1K_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum] |
|
2.35e-232 | 3 | 544 | 8 | 560 | Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHU_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHV_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHV_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHZ_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1AHZ_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],1VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],2VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum],2VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum] |
|
2.35e-232 | 3 | 544 | 8 | 560 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.21e-231 | 3 | 544 | 8 | 560 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
|
9.31e-115 | 6 | 532 | 8 | 515 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
|
2.14e-15 | 68 | 280 | 43 | 231 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
|
8.00e-13 | 28 | 529 | 91 | 559 | D-lactate dehydrogenase [cytochrome], mitochondrial OS=Arabidopsis thaliana OX=3702 GN=DLD PE=1 SV=1 |
|
4.75e-11 | 68 | 311 | 68 | 309 | Probable D-lactate dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=LDHD PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000066 | 0.000001 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.