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CAZyme Information: KIW10845.1

You are here: Home > Sequence: KIW10845.1

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 spinifera
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala spinifera
CAZyme ID KIW10845.1
CAZy Family AA3
CAZyme Description FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0D2AWI2]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
603 KN847499|CGC3 66513.67 7.3815
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EspiniferaCBS89968 12110 N/A 61 12049
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 52 590 7.2e-198 0.9923371647509579

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 1.26e-28 110 250 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 1.19e-25 87 578 9 455
FAD/FMN-containing dehydrogenase [Energy production and conversion].
178402 PLN02805 6.30e-08 93 253 120 274
D-lactate dehydrogenase [cytochrome]
183043 PRK11230 2.50e-05 113 258 59 205
glycolate oxidase subunit GlcD; Provisional
273750 pln_FAD_oxido 0.002 110 201 32 123
plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.36e-290 5 591 9 592
7.58e-248 5 591 6 590
8.87e-230 141 591 1 447
1.31e-223 10 591 12 585
1.99e-223 1 591 1 582

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.51e-168 49 591 8 559
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]
3.62e-167 49 591 8 559
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]
3.62e-167 49 591 8 559
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum],1W1L_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum]
3.62e-167 49 591 8 559
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]
1.45e-166 49 591 8 559
Structure of the Y503F mutant of vanillyl alcohol oxidase [Penicillium simplicissimum],5MXU_B Structure of the Y503F mutant of vanillyl alcohol oxidase [Penicillium simplicissimum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.86e-166 49 591 8 559
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
2.20e-106 46 580 2 515
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
5.08e-12 112 397 43 308
Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
1.07e-10 61 290 106 319
D-lactate dehydrogenase [cytochrome] 1, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DLD1 PE=1 SV=2
1.23e-10 64 298 30 265
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
1.000031 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KIW10845.1.