CAZyme Information: FPRO_05481-t41_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRO_05481-t41_1-p1
• CAZy Family: CE16
• CAZyme Description: related to 6-hydroxy-D-nicotine oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
489	FJOF01000004|CGC1	55647.61	7.3773

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=FJOF01000004:3899119-3900708(+)

Full Sequence      

MADDRFYTTTPKYSKKVLNQGDPDYEKCRRMNPTAHKIERFPAEIHIPETPAEVAKALAR
ATELGVPIGVRSSGHIFHFPALWHGGILIDAVNLNRRIDYDPVTKEICFGPSSRVEELAA
KLKEVNRFFPHGHAPTVGSAGFMLAGGQGWFVRGWGATNQTWITKIEMVVPDGRTLIASR
TENQDLFWAARGSGMGFFAVVTRFWGRTIERSTMWEKTLKFVINDDNYMALMSWAIERGR
DTPKYGTDLNLTIDYREKYDPAYTTDDVPPNATLVLTLNNLCYTDTQREARTLLSAYDRI
TPEVADFLIESKPVQVRTFEEVFARKRTFLGNAGQERWSINSIMNDPDVPLARLLEGIRP
AMLKLPTRVSSVFICHCDIKPDEDDACLSLPQDLYISTLTGWTDPKLEPAIMQPMRDYYR
QAFPVAVGQYITDIDINCEDANSKVMSDTALAKFLRIREKYDPKELFPTYKAFVKTSEKI
NKLQNKSRL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	35	467	1e-50	0.9694323144104804

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	7.57e-25	24	473	14	456	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	4.76e-19	42	179	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.
273750	pln_FAD_oxido	2.22e-06	23	226	25	223	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA72155.1|AA7	1.13e-16	37	202	90	270
ANF89368.1|AA7	1.69e-16	32	239	42	264
AEO58513.1|AA7|1.1.3.-	1.69e-16	32	239	42	264
QUC19098.1|AA7	2.03e-15	42	208	48	214
UNI23960.1|AA7	6.46e-15	42	208	48	214

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5K8E_A	5.83e-18	32	239	42	264	Xylooligosaccharide oxidase from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],5L6F_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose [Thermothelomyces thermophilus ATCC 42464],5L6G_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylose [Thermothelomyces thermophilus ATCC 42464]
6FYE_A	2.15e-17	16	204	21	204	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	5.10e-17	16	204	21	204	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
6FYG_A	1.21e-16	16	204	21	204	The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
6FYF_A	1.21e-16	16	204	21	204	The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A2I6PJ02|NODO_HYPPI	6.39e-27	24	463	21	436	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	7.71e-23	17	237	11	228	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A0E3D8N0|JANO_PENJA	2.52e-22	19	463	13	435	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	8.37e-22	17	237	11	228	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|G2QG48|XYLO_MYCTT	3.00e-17	32	239	42	264	Xylooligosaccharide oxidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=xylO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000079	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FPRO_05481-t41_1-p1.