dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: FPRN_05344-t42_1-p1

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Basic Information help

Species

Fusarium proliferatum

Lineage

Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum

CAZyme ID

FPRN_05344-t42_1-p1

CAZy Family

CE3

CAZyme Description

uncharacterized protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
572		64450.52	6.8079

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FproliferatumNRRL62905	15602	N/A	348	15254

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in FPRN_05344-t42_1-p1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA4	32	559	1.4e-126	0.9885057471264368

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	5.93e-32	85	224	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	8.33e-31	49	550	1	455	FAD/FMN-containing dehydrogenase [Energy production and conversion].
183043	PRK11230	8.90e-12	43	331	5	287	glycolate oxidase subunit GlcD; Provisional
178402	PLN02805	5.04e-11	84	268	133	308	D-lactate dehydrogenase [cytochrome]
397178	FAD-oxidase_C	4.82e-05	479	549	172	247	FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
7.70e-310	1	568	1	573
8.01e-255	1	562	1	567
3.42e-234	1	567	1	575
1.08e-215	1	536	1	544
1.97e-215	1	559	1	565

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.83e-96	32	558	3	522	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]
7.68e-89	32	559	4	528	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]
1.06e-80	34	560	12	556	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]
1.49e-80	34	560	12	556	Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
2.09e-80	34	560	12	556	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.95e-79	34	560	12	556	Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
3.26e-78	34	552	9	515	4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
6.96e-16	75	307	31	253	Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
2.43e-15	42	299	31	275	Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1
2.77e-14	47	315	11	264	Lactate dehydrogenase (NAD(+),ferredoxin) subunit LctD OS=Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1) OX=931626 GN=lctD PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000069	0.000000

TMHMM Annotations help

There is no transmembrane helices in FPRN_05344-t42_1-p1.