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CAZyme Information: ZTRI_3.893.mRNA-p1

You are here: Home > Sequence: ZTRI_3.893.mRNA-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 Zymoseptoria tritici
Lineage Ascomycota; Dothideomycetes; ; Mycosphaerellaceae; Zymoseptoria; Zymoseptoria tritici
CAZyme ID ZTRI_3.893.mRNA-p1
CAZy Family GH43
CAZyme Description similar to FAD binding domain-containing protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
503 54538.35 4.7953
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_ZtriticiIPO323 11839 336722 13 11826
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 73 288 8.5e-56 0.46943231441048033

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 1.52e-16 75 210 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.
223354 GlcD 1.60e-11 65 492 21 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658 BBE 1.05e-05 457 492 2 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.
215242 PLN02441 2.20e-05 74 233 64 233
cytokinin dehydrogenase
273751 FAD_lactone_ox 0.002 66 243 4 183
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.70e-24 50 492 14 464
9.99e-24 14 252 7 241
6.53e-23 72 492 59 489
9.19e-21 73 240 61 230
1.20e-20 73 236 71 236

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.31e-24 72 492 40 470
Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
2.31e-24 72 492 40 470
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]
1.88e-23 44 237 17 207
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]
3.40e-23 44 237 17 207
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]
3.40e-23 44 237 17 207
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
7.28e-78 38 502 9 476
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
1.73e-76 38 502 45 513
FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
1.50e-71 63 502 67 517
FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
3.35e-56 75 502 67 507
FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
3.35e-56 75 502 67 507
FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000267 0.999684 CS pos: 20-21. Pr: 0.9715

TMHMM  Annotations      help

There is no transmembrane helices in ZTRI_3.893.mRNA-p1.