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CAZyme Information: KAB8205741.1

You are here: Home > Sequence: KAB8205741.1

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 Aspergillus parasiticus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus parasiticus
CAZyme ID KAB8205741.1
CAZy Family GH18
CAZyme Description FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A5N6DKX0]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
512 ML734968|CGC2 56115.31 6.0604
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AparasiticusCBS117618 14005 N/A 253 13752
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in KAB8205741.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 71 272 1.7e-51 0.4410480349344978

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 1.03e-20 44 506 2 457
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 2.09e-17 76 204 5 135
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.
215242 PLN02441 1.99e-06 76 230 69 232
cytokinin dehydrogenase
273751 FAD_lactone_ox 2.55e-06 77 239 20 181
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.
178402 PLN02805 8.12e-06 76 235 138 303
D-lactate dehydrogenase [cytochrome]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.73e-19 73 275 91 294
1.88e-16 101 504 92 488
4.89e-16 78 235 79 237
5.52e-16 78 275 43 225
5.59e-16 71 235 47 212

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.11e-25 79 232 52 204
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]
5.65e-25 79 232 52 204
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]
5.65e-25 79 232 52 204
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-24 79 232 52 204
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]
1.03e-24 79 232 52 204
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T 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
1.95e-76 63 501 70 509
FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
4.89e-59 71 511 80 513
FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
2.77e-57 49 511 24 476
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
8.68e-42 73 511 96 514
Bifunctional solanapyrone synthase OS=Alternaria solani OX=48100 GN=sol5 PE=1 SV=1
1.27e-41 71 498 91 504
FAD-dependent monooxygenase macF OS=Penicillium terrestre OX=374132 GN=macF PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000234 0.999726 CS pos: 22-23. Pr: 0.8928

TMHMM  Annotations      help

There is no transmembrane helices in KAB8205741.1.