CAZyme Information: FPRO_06986-t41_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRO_06986-t41_1-p1
• CAZy Family: GH12
• CAZyme Description: related to 4-cresol dehydrogenase flavoprotein subunit

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
541		59091.21	6.2003

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FproliferatumET1	16509	1227346	366	16143

• Gene Location: location=FJOF01000003:570025-571768(-)

Full Sequence      

MSSSPKVLPPGIGPSEHRQFFDELAKVVGDENISRDASTGALVGPHQQQSYGDPYAIANQ
DQHLPSGAVRPASVQELQQVLRLANELSVPLWTVSRGRNLGYGGSAPAVAGSVVLDLHRM
NRIVEVNEADAYAIVEPGVSFFDLYEEIKRRDLALWPSCAAIGWGSVVGNTLDHGFGYTP
DGVHTEAQCGMEVVLPTGELLRTGMGAMTDSRLFPLYKAGFGPSVDGLFYQSNLGVVTKL
GIHITPAPEAYTACELSVPNETDLPQLVELLASLQRRGVVTNHPSISNVFRQAILSPNEA
VKAKLATHFGPGKAVPESVLDELKSNQCWGFWRAEFGLQGDADVVPALESSLRRAMAKIP
GARLETRQFGGTPGEFLRADKVETRGIPHNGVPTLEALSLMDYRLAAGSGHTDFAPVLPT
SGPELLEWYLAAKEMVSEAKFDFFADFHAYSRYIIPIILIVYTPEEKERAKELCQKLIDD
AFHRGLTTYRTHVEFMDQIRSHFSYKEHALAKLVDSFKATMDPKNILSPGKSGIARAKQK
I

Enzyme Prediction     

No EC number prediction in FPRO_06986-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA4	5	537	1.7e-151	0.9827586206896551

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	9.19e-34	65	204	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	3.92e-27	23	532	1	455	FAD/FMN-containing dehydrogenase [Energy production and conversion].
178402	PLN02805	1.23e-09	18	279	96	352	D-lactate dehydrogenase [cytochrome]
183043	PRK11230	1.98e-08	64	249	55	232	glycolate oxidase subunit GlcD; Provisional
273751	FAD_lactone_ox	5.01e-06	65	201	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
QPC60773.1|AA4	0.0	1	534	1	534
CEF88561.1|AA4	0.0	1	534	1	534
CZS83222.1|AA4	0.0	1	534	1	534
BCS19452.1|AA4	5.89e-212	20	538	18	534
VBB73832.1|AA4	4.71e-200	8	534	1	524

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FXD_A	2.58e-112	6	534	3	516	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]
1E0Y_A	2.18e-103	5	534	9	548	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]
1DZN_A	6.08e-103	5	534	9	548	Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
1AHU_A	8.57e-103	5	534	9	548	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]
1W1M_A	1.21e-102	5	534	9	548	STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Glu502Gly Mutant [Penicillium simplicissimum],1W1M_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Glu502Gly Mutant [Penicillium simplicissimum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P56216|VAOX_PENSI	4.41e-102	5	534	9	548	Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
sp|P09788|DH4C_PSEPU	3.44e-89	7	534	8	515	4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
sp|P94535|GLCD_BACSU	2.63e-18	22	249	8	218	Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
sp|P9WIT0|Y2280_MYCTO	5.85e-16	24	246	8	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	5.85e-16	24	246	8	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
1.000063	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FPRO_06986-t41_1-p1.