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CAZyme Information: EJT74189.1

You are here: Home > Sequence: EJT74189.1

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 Gaeumannomyces tritici
Lineage Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici
CAZyme ID EJT74189.1
CAZy Family GH15
CAZyme Description FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:J3P3E7]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
551 61683.31 8.9391
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_GtriticiR3-111a-1 14749 644352 291 14458
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 37 254 1.5e-64 0.4344978165938865

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 1.80e-33 39 181 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.
223354 GlcD 1.28e-29 25 455 19 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658 BBE 2.31e-11 416 462 1 45
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.
273751 FAD_lactone_ox 1.01e-05 39 216 15 178
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 2.90e-04 35 209 61 231
cytokinin dehydrogenase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.99e-26 18 215 42 227
5.32e-22 39 256 64 268
5.32e-22 39 256 64 268
2.29e-21 39 256 64 268
3.58e-21 18 231 144 346

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.80e-22 38 225 53 230
Crystal structure of tetrahydrocannabinolic acid synthase from Cannabis sativa [Cannabis sativa]
1.17e-21 15 219 22 211
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
2.80e-21 15 219 22 211
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]
5.02e-21 15 219 22 211
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]
5.02e-21 15 219 22 211
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.21e-26 22 461 17 442
Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
2.78e-23 25 216 115 305
FAD-linked oxidoreductase easE OS=Trichophyton verrucosum (strain HKI 0517) OX=663202 GN=easE PE=3 SV=1
1.73e-22 25 216 27 217
FAD-linked oxidoreductase easE OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=easE PE=3 SV=1
2.08e-22 38 468 76 533
Berberine bridge enzyme-like 12 OS=Arabidopsis thaliana OX=3702 GN=At1g30740 PE=2 SV=1
3.70e-22 39 216 14 190
FAD-linked oxidoreductase easE OS=Claviceps purpurea OX=5111 GN=easE PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000090 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in EJT74189.1.