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CAZyme Information: GBF62316.1

You are here: Home > Sequence: GBF62316.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Trichophyton mentagrophytes
Lineage Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes
CAZyme ID GBF62316.1
CAZy Family GH16
CAZyme Description FAD-linked oxidoreductase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
467 BFBS01016074|CGC1 50803.46 4.7219
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_TmentagrophytesTIMM2789 7958 N/A 98 7860
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 48 260 7.4e-40 0.4868995633187773

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 2.90e-17 52 457 27 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 8.32e-10 57 182 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.
369658 BBE 7.13e-07 422 457 1 38
Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.99e-18 75 465 76 470
1.67e-17 57 458 58 479
4.60e-17 49 457 55 489
2.52e-16 54 465 171 594
2.59e-16 61 466 80 494

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.02e-23 56 465 54 461
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]
1.38e-23 56 465 54 461
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]
1.86e-23 56 465 54 461
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
2.51e-23 56 465 54 461
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]
3.38e-23 56 465 54 461
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.66e-62 39 467 55 506
FAD-linked oxidoreductase OXR1 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR1 PE=1 SV=1
4.62e-51 48 462 65 492
FAD-linked oxidoreductase srdI OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=srdI PE=2 SV=1
3.24e-49 12 463 17 480
FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1
2.89e-48 24 457 43 501
FAD-linked oxidoreductase virI OS=Hypocrea virens (strain Gv29-8 / FGSC 10586) OX=413071 GN=virI PE=3 SV=1
3.35e-48 28 457 36 493
FAD-linked oxidoreductase chyH OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=chyH PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000367 0.999600 CS pos: 19-20. Pr: 0.9452

TMHMM  Annotations      help

There is no transmembrane helices in GBF62316.1.