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CAZyme Information: GBF66235.1

You are here: Home > Sequence: GBF66235.1

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 GBF66235.1
CAZy Family GT34
CAZyme Description D-arabinono-1,4-lactone oxidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
570 63645.20 5.8997
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.-:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 28 236 1.4e-27 0.4606986899563319

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
273751 FAD_lactone_ox 1.14e-147 29 473 7 436
sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
397924 ALO 2.17e-111 197 480 2 259
D-arabinono-1,4-lactone oxidase. This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.
223354 GlcD 4.39e-43 36 472 31 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
215258 PLN02465 1.95e-39 29 485 89 573
L-galactono-1,4-lactone dehydrogenase
396238 FAD_binding_4 7.56e-36 37 172 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.07e-11 37 195 62 223
2.01e-10 82 195 121 234
2.18e-10 37 203 58 229
5.96e-10 28 203 52 229
7.52e-10 16 231 49 270

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.44e-27 24 260 110 348
Assembly intermediate of the plant mitochondrial complex I [Brassica oleracea]
1.38e-15 29 206 13 186
Alditol Oxidase from Streptomyces coelicolor A3(2): Native Enzyme [Streptomyces coelicolor A3(2)],2VFS_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Xylitol [Streptomyces coelicolor A3(2)],2VFT_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sorbitol [Streptomyces coelicolor A3(2)],2VFU_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Mannitol [Streptomyces coelicolor A3(2)],2VFV_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sulphite [Streptomyces coelicolor A3(2)]
1.44e-10 37 197 48 212
Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
1.44e-10 37 197 48 212
Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
1.45e-10 29 202 46 228
Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPN_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPP_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPP_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPQ_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPQ_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPT_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPT_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPU_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPU_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPX_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPX_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.13e-202 13 521 27 548
Putative D-arabinono-1,4-lactone oxidase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=alo-1 PE=3 SV=1
2.47e-132 20 482 9 525
D-arabinono-1,4-lactone oxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALO1 PE=3 SV=1
1.35e-115 17 480 10 552
D-arabinono-1,4-lactone oxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALO1 PE=1 SV=1
2.47e-112 22 473 14 513
D-arabinono-1,4-lactone oxidase OS=Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OX=284811 GN=ALO1 PE=3 SV=1
8.81e-111 18 473 6 509
D-arabinono-1,4-lactone oxidase OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=ALO1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000056 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in GBF66235.1.