Species | Campylobacter sp900753405 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Campylobacteraceae; Campylobacter; Campylobacter sp900753405 | |||||||||||
CAZyme ID | MGYG000001044_00343 | |||||||||||
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: 50029; End: 51585 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 3 | 516 | 1.7e-206 | 0.9865900383141762 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam01565 | FAD_binding_4 | 1.85e-30 | 55 | 195 | 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. |
COG0277 | GlcD | 4.20e-29 | 21 | 509 | 1 | 455 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
PRK11230 | PRK11230 | 3.05e-14 | 13 | 304 | 14 | 288 | glycolate oxidase subunit GlcD; Provisional |
PLN02805 | PLN02805 | 2.26e-13 | 54 | 254 | 133 | 323 | D-lactate dehydrogenase [cytochrome] |
pfam02913 | FAD-oxidase_C | 4.14e-10 | 407 | 508 | 145 | 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 |
---|---|---|---|---|---|
CCD51118.1 | 1.51e-143 | 4 | 517 | 29 | 578 |
ATZ45204.1 | 6.02e-143 | 4 | 517 | 29 | 578 |
APA07334.1 | 8.00e-143 | 4 | 517 | 29 | 578 |
QSZ30937.1 | 2.34e-136 | 4 | 517 | 29 | 578 |
AFJ11909.1 | 7.79e-134 | 4 | 511 | 7 | 543 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1WVE_A | 3.00e-217 | 6 | 514 | 8 | 517 | 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] |
1DII_A | 3.11e-217 | 6 | 514 | 9 | 518 | 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] |
5FXD_A | 1.43e-134 | 5 | 511 | 4 | 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] |
1E0Y_A | 1.67e-130 | 4 | 511 | 10 | 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] |
1W1L_A | 2.36e-130 | 4 | 511 | 10 | 548 | STRUCTUREOF 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 |
---|---|---|---|---|---|---|
P09788 | 1.70e-216 | 6 | 514 | 9 | 518 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
P56216 | 5.15e-129 | 4 | 511 | 10 | 548 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
F1QXM5 | 6.25e-17 | 13 | 250 | 30 | 258 | Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1 |
P94535 | 7.42e-17 | 54 | 272 | 40 | 247 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
Q94AX4 | 2.13e-13 | 54 | 508 | 145 | 559 | D-lactate dehydrogenase [cytochrome], mitochondrial OS=Arabidopsis thaliana OX=3702 GN=DLD PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000053 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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