Species | Helicobacter_B sp001854545 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Helicobacteraceae; Helicobacter_B; Helicobacter_B sp001854545 | |||||||||||
CAZyme ID | MGYG000002443_01670 | |||||||||||
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: 3509; End: 5185 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 2 | 538 | 6.2e-139 | 0.9885057471264368 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam01565 | FAD_binding_4 | 5.52e-31 | 54 | 194 | 1 | 138 | 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 | 2.79e-29 | 19 | 527 | 2 | 454 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
PLN02805 | PLN02805 | 1.09e-16 | 53 | 254 | 133 | 323 | D-lactate dehydrogenase [cytochrome] |
PRK11230 | PRK11230 | 3.56e-06 | 33 | 240 | 47 | 232 | glycolate oxidase subunit GlcD; Provisional |
TIGR01676 | GLDHase | 4.69e-04 | 30 | 144 | 31 | 148 | galactonolactone dehydrogenase. This model represents L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3). This enzyme catalyzes the final step in ascorbic acid biosynthesis in higher plants. This protein is homologous to ascorbic acid biosynthesis enzymes of other species: L-gulono-gamma-lactone oxidase in rat and L-galactono-gamma-lactone oxidase in yeast. All three covalently bind the cofactor FAD. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGA17285.1 | 3.37e-100 | 2 | 531 | 50 | 572 |
QKX53028.1 | 1.25e-98 | 2 | 538 | 54 | 587 |
BCS28313.1 | 2.31e-98 | 3 | 535 | 58 | 586 |
QGA13141.1 | 1.08e-96 | 3 | 537 | 35 | 565 |
CDR40370.1 | 2.58e-96 | 3 | 533 | 46 | 569 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5FXD_A | 3.29e-104 | 3 | 533 | 5 | 519 | 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] |
1WVE_A | 2.31e-95 | 2 | 530 | 7 | 514 | 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 | 2.37e-95 | 2 | 530 | 8 | 515 | 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] |
1W1K_A | 3.49e-95 | 1 | 537 | 10 | 555 | STRUCTUREOF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum],1W1K_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum] |
1W1L_A | 1.36e-94 | 1 | 537 | 10 | 555 | 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 | 1.30e-94 | 2 | 530 | 8 | 515 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
P56216 | 1.05e-93 | 1 | 537 | 10 | 555 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
P94535 | 2.77e-20 | 33 | 253 | 20 | 231 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
D4MUV9 | 2.15e-16 | 33 | 259 | 38 | 243 | D-lactate dehydrogenase OS=Anaerostipes hadrus OX=649756 GN=CL2_23160 PE=1 SV=1 |
A4VGK4 | 1.51e-15 | 40 | 260 | 27 | 238 | 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 |
---|---|---|---|---|---|
1.000056 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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