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CAZyme Information: EPrPAT00000024444-p1

You are here: Home > Sequence: EPrPAT00000024444-p1

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 Pythium aphanidermatum
Lineage Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
CAZyme ID EPrPAT00000024444-p1
CAZy Family GT71
CAZyme Description FAD-binding protein.
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
332 PaphDAOMBR444_SC1025|CGC1 35622.54 7.5081
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444 12363 1223555 58 12305
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 59 290 1.7e-78 0.49344978165938863

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 1.55e-22 63 273 25 238
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 7.63e-21 70 211 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.
273751 FAD_lactone_ox 5.43e-06 70 274 15 220
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.
215242 PLN02441 8.10e-06 70 244 65 242
cytokinin dehydrogenase
178402 PLN02805 4.42e-05 70 244 134 308
D-lactate dehydrogenase [cytochrome]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.14e-45 59 297 109 347
1.17e-43 51 295 40 287
5.53e-43 63 295 114 344
9.53e-43 51 314 43 304
1.12e-42 53 295 46 286

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.51e-44 51 314 24 285
The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum]
6.81e-43 51 314 24 285
Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
1.54e-42 60 315 51 303
Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
2.68e-39 40 277 15 245
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]
3.73e-39 40 277 15 245
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.19e-46 44 313 49 314
FAD-linked oxidoreductase pynB OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pynB PE=1 SV=1
7.30e-45 53 295 46 286
FAD-linked oxidoreductase subF OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=subF PE=3 SV=1
1.97e-44 53 295 46 286
FAD-linked oxidoreductase dpmaF OS=Metarhizium anisopliae OX=5530 GN=dpmaF PE=1 SV=1
1.69e-43 51 314 43 304
Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1
8.01e-43 46 332 40 321
FAD-linked oxidoreductase pytB OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pytB PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.069546 0.930450 CS pos: 18-19. Pr: 0.7459

TMHMM  Annotations      help

There is no transmembrane helices in EPrPAT00000024444-p1.