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CAZyme Information: KEF53785.1

You are here: Home > Sequence: KEF53785.1

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 Exophiala aquamarina
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala aquamarina
CAZyme ID KEF53785.1
CAZy Family CBM21
CAZyme Description FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A072PE31]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
591 65980.26 6.1357
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EaquamarinaCBS119918 13118 1182545 0 13118
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.38:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA4 40 587 2e-245 0.9961685823754789

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 3.20e-27 103 244 2 139
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 3.51e-23 80 575 8 455
FAD/FMN-containing dehydrogenase [Energy production and conversion].
178402 PLN02805 5.50e-12 63 574 77 547
D-lactate dehydrogenase [cytochrome]
397178 FAD-oxidase_C 7.05e-12 345 574 15 247
FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.
183043 PRK11230 6.78e-07 105 325 59 254
glycolate oxidase subunit GlcD; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 39 589 8 558
1.02e-317 39 589 5 555
1.02e-317 39 589 5 555
2.03e-317 39 589 5 555
5.96e-315 39 589 5 555

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.64e-272 40 589 9 560
Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form [Penicillium simplicissimum],1E8F_B Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form [Penicillium simplicissimum],1E8G_A STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL [Penicillium simplicissimum],1E8G_B STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL [Penicillium simplicissimum],1E8H_A Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form Complexed By Adp [Penicillium simplicissimum],1E8H_B Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form Complexed By Adp [Penicillium simplicissimum]
3.82e-271 40 589 9 560
Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
7.69e-271 40 589 9 560
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum],1W1K_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum]
7.69e-271 40 589 9 560
Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHU_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHV_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHV_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHZ_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1AHZ_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],1VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],2VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum],2VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum]
1.55e-270 40 589 9 560
STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE [Penicillium simplicissimum],1QLT_B STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE [Penicillium simplicissimum],1QLU_A Structure Of The H422a Mutant Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum],1QLU_B Structure Of The H422a Mutant Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.96e-270 40 589 9 560
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
4.89e-115 43 577 9 515
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
5.59e-14 53 574 29 482
Probable D-lactate dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Ldhd PE=1 SV=1
1.62e-13 101 574 145 559
D-lactate dehydrogenase [cytochrome], mitochondrial OS=Arabidopsis thaliana OX=3702 GN=DLD PE=1 SV=1
5.73e-13 53 357 29 314
Probable D-lactate dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=LDHD PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000054 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KEF53785.1.