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CAZyme Information: CC1G_11355-t26_1-p1

You are here: Home > Sequence: CC1G_11355-t26_1-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 Coprinopsis cinerea
Lineage Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
CAZyme ID CC1G_11355-t26_1-p1
CAZy Family GT15
CAZyme Description FAD binding domain-containing protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
579 AACS02000011|CGC9 62709.93 4.4128
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ccinereaokay7-130 13657 240176 301 13356
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 134 359 1.7e-51 0.45414847161572053

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 5.12e-23 134 278 7 139
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 2.39e-18 127 559 31 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658 BBE 1.79e-07 522 566 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.82e-53 27 574 500 1058
1.82e-53 27 574 500 1058
7.94e-15 128 567 70 497
9.61e-13 135 566 72 490
2.94e-12 127 565 62 483

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.33e-74 27 578 28 571
Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
1.53e-53 8 570 9 587
Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
7.72e-18 100 559 32 453
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
1.03e-17 100 559 32 453
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]
1.03e-17 100 559 32 453
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.60e-111 8 577 7 587
Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07056 PE=1 SV=2
4.65e-92 8 568 9 560
Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02478 PE=1 SV=1
2.38e-81 9 576 7 576
FAD-linked oxidoreductase malF OS=Malbranchea aurantiaca OX=78605 GN=malF PE=1 SV=1
2.94e-76 8 578 11 574
FAD-linked oxidoreductase penH OS=Penicillium thymicola OX=293382 GN=penH PE=1 SV=1
1.63e-75 8 578 11 589
FAD-linked oxidoreductase notD OS=Aspergillus sp. (strain MF297-2) OX=877550 GN=notD PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000189 0.999785 CS pos: 18-19. Pr: 0.9808

TMHMM  Annotations      help

There is no transmembrane helices in CC1G_11355-t26_1-p1.