Species | Gaeumannomyces tritici | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici | |||||||||||
CAZyme ID | EJT69416.1 | |||||||||||
CAZy Family | AA2 | |||||||||||
CAZyme Description | FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:J3PHQ4] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 133 | 337 | 4.3e-50 | 0.425764192139738 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 1.03e-23 | 137 | 273 | 1 | 136 | 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 | 2.94e-21 | 137 | 307 | 32 | 205 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
215242 | PLN02441 | 6.27e-12 | 117 | 300 | 46 | 233 | cytokinin dehydrogenase |
178402 | PLN02805 | 2.68e-04 | 137 | 299 | 134 | 298 | D-lactate dehydrogenase [cytochrome] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
8.34e-25 | 112 | 309 | 37 | 230 | |
6.49e-23 | 131 | 565 | 64 | 514 | |
1.32e-21 | 137 | 557 | 63 | 478 | |
9.37e-21 | 112 | 323 | 24 | 230 | |
9.37e-21 | 112 | 323 | 24 | 230 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.27e-21 | 100 | 557 | 10 | 454 | The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus] |
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2.26e-21 | 100 | 557 | 10 | 454 | The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus] |
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2.26e-21 | 100 | 557 | 10 | 454 | The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus] |
|
2.26e-21 | 100 | 557 | 10 | 454 | The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus] |
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4.05e-21 | 100 | 557 | 10 | 454 | The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.15e-66 | 112 | 566 | 57 | 524 | FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1 |
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1.60e-61 | 111 | 566 | 56 | 513 | FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1 |
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2.00e-61 | 114 | 566 | 56 | 517 | FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1 |
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1.47e-59 | 125 | 566 | 2 | 456 | FAD-dependent monooxygenase CTB5 OS=Cercospora nicotianae OX=29003 GN=CTB5 PE=2 SV=1 |
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3.40e-56 | 94 | 566 | 2 | 476 | FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000065 | 0.000000 |
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