CAZyme Information: ASPWEDRAFT_42410-t33_1-p1

Basic Information

• Species: Aspergillus wentii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus wentii
• CAZyme ID: ASPWEDRAFT_42410-t33_1-p1
• CAZy Family: GH7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
434		49474.58	6.3175

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AwentiiDTO134E9	12659	1073089	224	12435

• Gene Location: location=KV878213:2016390-2017997(+)

Full Sequence      

MNRILEVNVEGAYVLLEPGVTYMDLHQYLVWNGLREKLWIDVPELGGGSILGNAVERGVG
YTPYGDHWMMHCGMEVVLPTGELLRTGMGAMPERDSSGDEKTRPDEEPGNKCWQLFPYGY
GPYNDGLFSQSNLGIVTKMGVWLMPNPGGFQSYLVTIPREEDLHQAVEIIRPLRVQLVLQ
NVPSIRHILLDAAMMRNKSEWTSSTNPIDDEGLDEISKSLNLGRWNFYGALYGPESVRNN
LWQIIKQSFSAIKGAKFYFPEDIREHCVLHIQNLTLQGIPNNEELKWVQWLPNGAHVSFS
PISKISGDDARSLYSIVKRRCNEAGFDYIATFTIGMREMHHILCIVFDREDPIMRRKAHQ
LIKTLIKDCAAHGWGEYRTHLGLMDQIAETYNWNDNALMRFNQTIKNTLDPNGILAPGKS
GIWPAVYDRNKYKM

Enzyme Prediction     

EC	1.1.3.38:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA4	1	431	1.6e-206	0.789272030651341

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	4.26e-13	1	87	53	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	4.18e-12	1	420	84	455	FAD/FMN-containing dehydrogenase [Energy production and conversion].
397178	FAD-oxidase_C	1.54e-09	301	419	136	247	FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.
178402	PLN02805	1.27e-04	1	419	187	547	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS20269.1|AA4	1.02e-242	1	434	125	557
EKG15142.1|AA4	4.66e-236	1	434	122	555
QKX53333.1|AA4	1.59e-231	1	432	139	570
CCD51118.1|AA4	8.24e-231	1	434	146	579
ATZ45204.1|AA4	8.24e-231	1	434	146	579

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1E8F_A	1.32e-230	1	434	127	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]
1DZN_A	2.67e-230	1	434	127	560	Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
1W1L_A	5.37e-230	1	434	127	560	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]
1W1K_A	2.18e-229	1	434	127	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]
1AHU_A	2.18e-229	1	434	127	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P56216|VAOX_PENSI	1.12e-228	1	434	127	560	Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
sp|P09788|DH4C_PSEPU	2.74e-90	1	422	113	515	4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
sp|Q94AX4|DLD_ARATH	1.84e-07	1	419	199	559	D-lactate dehydrogenase [cytochrome], mitochondrial OS=Arabidopsis thaliana OX=3702 GN=DLD PE=1 SV=1
sp|Q86WU2|LDHD_HUMAN	3.76e-06	1	419	119	505	Probable D-lactate dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=LDHD PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000063	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ASPWEDRAFT_42410-t33_1-p1.