CAZyme Information: ASPNIDRAFT2_1079445-t41_1-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: ASPNIDRAFT2_1079445-t41_1-p1
• CAZy Family: AA1
• CAZyme Description: Vanillyl alcohol oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
552		60591.89	6.3619

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerATCC1015	11910	380704	6	11904

• Gene Location: location=ACJE01000001.1:331376-333266(+)

Full Sequence      

MAQPTKRILPLLLEESTFDKVLDKLSEIVGEPNFSRNHLYGNLEGPQGQNCYDDLWPLGN
PTDHTPSGAVRPKTVNEIQQVLQIANEYKLPLWTVSRGRNLGYGGSGAIVPGSVILDLHR
MDKIIEVNEEFAYAIVEPGVSFFGLYEYIQDRGYRLWPSCPALGWGSIVGNTLDRGFGYT
PNGEHAEQQCGMEVVLATGEVLRTGMGALSGSPMWALYKGGYGPSVDGLFYQSNLGVVTK
IGIHLTPAPACFMDCVVSVPNEEDIGALVRIMSALEREGIVQNHASIANPYRQALSSEDP
LVLGRAVGPGIEGGYATNADMTKLAKEQGWGYWKAHFAIYGASGAFIDACWTIVQERFAA
IPGAAATAERHEHKLGGRLNAAELPMGEIPHTGYPCLTAKDFVDIRGAKGGHIAFSPLFP
PDGKQLQEWFSRIRPLVEKAGFDLFSDFHIHGRYIIGIVLVVYTPAEAARAKSLFDELLK
DGVERSSVSEYRTHIHFMDEVRRHYDWGNGILHRTLGSIRKTLDPNGILSQGKSGIWTSS
RPLTEAIRNTRL

Enzyme Prediction     

No EC number prediction in ASPNIDRAFT2_1079445-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA4	7	539	2.2e-143	0.9808429118773946

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	7.90e-31	66	205	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	9.46e-26	64	534	30	455	FAD/FMN-containing dehydrogenase [Energy production and conversion].
178402	PLN02805	1.78e-10	52	276	114	337	D-lactate dehydrogenase [cytochrome]
183043	PRK11230	1.47e-08	65	274	55	257	glycolate oxidase subunit GlcD; Provisional
273751	FAD_lactone_ox	4.18e-07	66	202	15	147	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS13142.1|AA4	0.0	1	552	1	552
BCS01400.1|AA4	0.0	1	552	1	552
BCS19452.1|AA4	3.27e-179	1	539	1	533
QPC60773.1|AA4	3.71e-176	1	536	1	534
CEF88561.1|AA4	5.26e-176	1	536	1	534

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FXD_A	5.83e-104	7	538	3	518	Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXD_B Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXE_A Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXE_B Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXF_A Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXF_B Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXP_A Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1],5FXP_B Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1]
1DII_A	1.97e-92	1	536	1	515	Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DII_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_A Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida]
1WVE_A	1.06e-91	2	536	1	514	p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVE_B p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVF_A p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida]
7PBG_A	1.13e-89	52	537	41	522	Chain A, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBG_B Chain B, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_A Chain A, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_B Chain B, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_C Chain C, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_D Chain D, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_E Chain E, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_F Chain F, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_G Chain G, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_H Chain H, FAD-binding oxidoreductase [Gulosibacter chungangensis]
1E0Y_A	4.83e-85	67	539	72	551	Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1E0Y_B Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09788|DH4C_PSEPU	1.01e-91	1	536	1	515	4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
sp|P56216|VAOX_PENSI	2.66e-83	67	539	72	551	Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
sp|P94535|GLCD_BACSU	1.44e-13	66	249	41	217	Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
sp|P9WIT0|Y2280_MYCTO	1.34e-12	24	247	7	213	Uncharacterized FAD-linked oxidoreductase MT2338 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT2338 PE=3 SV=1
sp|P9WIT1|Y2280_MYCTU	1.34e-12	24	247	7	213	Uncharacterized FAD-linked oxidoreductase Rv2280 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2280 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000092	0.000001

TMHMM  Annotations     

There is no transmembrane helices in ASPNIDRAFT2_1079445-t41_1-p1.