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CAZyme Information: ACLA_066010-t26_1-p1

You are here: Home > Sequence: ACLA_066010-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 Aspergillus clavatus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
CAZyme ID ACLA_066010-t26_1-p1
CAZy Family GH51
CAZyme Description FAD dependent oxidoreductase, putative
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
496 54400.49 5.0237
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AclavatusNRRL1 9428 344612 287 9141
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 59 276 1.4e-55 0.4737991266375546

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 5.32e-17 53 228 23 205
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 1.04e-14 62 198 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.
273751 FAD_lactone_ox 5.91e-06 68 231 21 183
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.
178402 PLN02805 8.83e-05 62 233 134 312
D-lactate dehydrogenase [cytochrome]
215242 PLN02441 0.002 180 220 192 232
cytokinin dehydrogenase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.53e-24 16 226 30 238
5.67e-22 62 485 48 464
5.67e-22 62 485 48 464
1.85e-21 62 485 48 464
2.17e-21 62 282 128 353

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.10e-20 48 290 32 257
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]
3.78e-20 48 290 32 257
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]
3.78e-20 48 290 32 257
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]
6.77e-20 48 290 32 257
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]
6.77e-20 48 290 32 257
Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_B Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_C Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_D Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],6FOQ_A The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_B The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_C The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_D The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOW_A The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_B The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_C The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_D The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FP3_A The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_B The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_C The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_D The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FY8_A The crystal structure of EncM bromide soak [Streptomyces maritimus],6FY9_A The crystal structure of EncM complex with xenon under 15 bars Xe pressure [Streptomyces maritimus],6FYA_A The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus],6FYA_B The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.71e-163 7 495 6 499
Uncharacterized FAD-linked oxidoreductase ARB_02372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02372 PE=1 SV=1
6.09e-52 20 495 56 514
Bifunctional solanapyrone synthase OS=Alternaria solani OX=48100 GN=sol5 PE=1 SV=1
7.08e-52 22 495 40 513
FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
5.74e-51 13 495 8 507
FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
5.74e-51 13 495 8 507
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
0.000219 0.999734 CS pos: 24-25. Pr: 0.9731

TMHMM  Annotations      help

There is no transmembrane helices in ACLA_066010-t26_1-p1.