Species | Pseudomonas citronellolis | |||||||||||
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Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas; Pseudomonas citronellolis | |||||||||||
CAZyme ID | MGYG000004151_04744 | |||||||||||
CAZy Family | AA4 | |||||||||||
CAZyme Description | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 25450; End: 27018 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 8 | 518 | 2.5e-206 | 0.9789272030651341 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0277 | GlcD | 1.94e-29 | 26 | 514 | 2 | 455 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
pfam01565 | FAD_binding_4 | 2.79e-29 | 59 | 199 | 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. |
PLN02805 | PLN02805 | 3.87e-12 | 20 | 513 | 96 | 547 | D-lactate dehydrogenase [cytochrome] |
PRK11230 | PRK11230 | 4.57e-11 | 20 | 514 | 19 | 471 | glycolate oxidase subunit GlcD; Provisional |
pfam02913 | FAD-oxidase_C | 1.64e-08 | 414 | 513 | 147 | 247 | FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
APA07334.1 | 3.83e-124 | 10 | 516 | 31 | 567 |
ATZ45204.1 | 1.14e-123 | 4 | 516 | 25 | 567 |
CCD51118.1 | 3.22e-123 | 4 | 516 | 25 | 567 |
QGI94813.1 | 8.10e-123 | 6 | 516 | 5 | 543 |
QGI63931.1 | 8.10e-123 | 6 | 516 | 5 | 543 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1DII_A | 0.0 | 6 | 522 | 5 | 521 | ChainA, 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] |
1WVE_A | 0.0 | 6 | 522 | 4 | 520 | p-CresolMethylhydroxylase: 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] |
5FXD_A | 1.08e-126 | 10 | 516 | 5 | 516 | Crystalstructure 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] |
7PBG_A | 2.98e-124 | 6 | 516 | 2 | 521 | ChainA, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBG_B Chain B, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_A Chain A, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_B Chain B, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_C Chain C, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_D Chain D, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_E Chain E, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_F Chain F, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_G Chain G, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_H Chain H, FAD-binding oxidoreductase [Gulosibacter chungangensis] |
1E0Y_A | 4.56e-113 | 10 | 516 | 12 | 548 | Structureof 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 |
---|---|---|---|---|---|---|
P09788 | 0.0 | 6 | 522 | 5 | 521 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
P56216 | 7.79e-111 | 10 | 516 | 12 | 548 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
P94535 | 1.79e-16 | 59 | 513 | 41 | 456 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
F1QXM5 | 4.47e-14 | 20 | 513 | 33 | 486 | Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1 |
A4VGK4 | 1.25e-13 | 25 | 195 | 9 | 176 | D-2-hydroxyglutarate dehydrogenase OS=Pseudomonas stutzeri (strain A1501) OX=379731 GN=d2hgdh PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000059 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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