CAZyme Information: FPRO_14558-t41_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRO_14558-t41_1-p1
• CAZy Family: GT109
• CAZyme Description: related to 6-hydroxy-D-nicotine oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
510	FJOF01000008|CGC20	57821.19	9.1682

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=FJOF01000008:2181751-2183496(-)

Full Sequence      

MMTLHLIFSFMLLTTLAVSSPLSVPPYFQPYHLTRREVPVFQIQQELGALLSENSLILLP
SNPLWLNTTKRWNTMAPPDIKVVVQPANEVDIPKIVSAWCTTINFLVVNRGHGLTKSLGA
FKGMQIDMKQLRSMNITRDGKSAWFQGGAYAYEVIPFLWDRGYVTSTGSNQCVGLTGPAL
GGGHGRYEGLYGLAGDNIVEMKVVLADGSSITVSDKSNKDLFWAMRGAGHNFGIVTNLKF
KIYPAKIKTWHYHNYYWRQDKLERVFRELNKLQDDGRTPPLLGVVFGQIYIDPSIRRDEA
ILWFTFAYAGPASEAERLLRPFNAIDAIKDEMGDVPYPEIPVRQNTDLSNCISAPFSLAS
VMLQTWNITTERALYNHFMRNVALYPDLAVTARLYYEGYAHRGVQAVDSASTAYSHRDEY
HIAFFATVVPEGSDLLGPAEKWAREARDMWYAGAPTRKPATYVNYASGNKYESLQSIYGY
ESWRLARLRKLKAKYDPHNRFRFYVPILSD

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	69	503	2.5e-55	0.982532751091703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	4.68e-19	81	214	2	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	2.93e-18	46	502	1	451	FAD/FMN-containing dehydrogenase [Energy production and conversion].
273751	FAD_lactone_ox	1.05e-04	85	245	20	181	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.
369658	BBE	0.002	461	503	1	40	Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UQC87672.1|AA7	2.23e-22	48	503	38	491
UPL01114.1|AA7	3.88e-22	111	502	95	483
QRW09115.1|AA7	1.02e-21	52	503	47	498
UQC82080.1|AA7	3.03e-19	61	503	30	471
QUC19098.1|AA7	3.88e-19	43	501	9	462

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO4_A	1.01e-21	107	503	74	464	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	1.82e-21	107	503	74	464	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6FYD_A	9.58e-21	57	502	22	454	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	1.28e-20	57	502	22	454	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]
6FYE_A	1.72e-20	57	502	22	454	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1J0KJK5|IACH_PESFW	1.86e-184	8	510	11	510	FAD-linked oxidoreductase iacH OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=iacH PE=1 SV=1
sp|G9N4A4|VIRI_HYPVG	4.84e-169	6	509	9	509	FAD-linked oxidoreductase virI OS=Hypocrea virens (strain Gv29-8 / FGSC 10586) OX=413071 GN=virI PE=3 SV=1
sp|G4N287|OXR2_MAGO7	4.22e-149	13	507	12	519	FAD-linked oxidoreductase OXR2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR2 PE=2 SV=1
sp|I1S3L1|CHRY5_GIBZE	4.87e-66	33	507	21	505	FAD-linked oxidoreductase chry5 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=chry5 PE=3 SV=1
sp|B6HLP5|CHYH_PENRW	3.86e-60	45	507	35	499	FAD-linked oxidoreductase chyH OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=chyH PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000233	0.999738	CS pos: 19-20. Pr: 0.9602

TMHMM  Annotations     

There is no transmembrane helices in FPRO_14558-t41_1-p1.