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CAZyme Information: FGRAMPH1_01T13987-p1

You are here: Home > Sequence: FGRAMPH1_01T13987-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 Fusarium graminearum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium graminearum
CAZyme ID FGRAMPH1_01T13987-p1
CAZy Family GH18
CAZyme Description fad linked oxidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
537 59208.39 5.0382
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FgraminearumPH-1 14145 229533 2 14143
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 44 479 7.9e-80 0.9716157205240175

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 1.78e-33 46 182 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 1.11e-32 13 482 2 459
FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658 BBE 3.95e-20 436 480 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.
215242 PLN02441 8.39e-16 37 196 58 220
cytokinin dehydrogenase
178402 PLN02805 4.14e-08 46 218 134 307
D-lactate dehydrogenase [cytochrome]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.57e-28 22 482 40 493
1.74e-27 19 479 37 489
4.91e-27 38 483 30 474
2.19e-26 13 482 130 595
2.71e-26 26 481 45 493

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.74e-34 21 483 21 463
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]
6.98e-34 21 483 21 463
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]
6.98e-34 21 483 21 463
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
9.52e-34 21 483 21 463
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]
1.30e-33 21 483 21 463
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
2.45e-43 46 482 33 445
Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
9.87e-36 21 481 9 445
Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1
6.89e-32 50 473 123 541
FAD-linked oxidoreductase ZEB1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=ZEB1 PE=2 SV=2
1.13e-30 40 483 65 520
Reticuline oxidase OS=Eschscholzia californica OX=3467 GN=BBE1 PE=1 SV=1
9.92e-30 40 482 70 540
Cannabichromenic acid synthase OS=Cannabis sativa OX=3483 GN=CBCAS PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000046 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in FGRAMPH1_01T13987-p1.