CAZyme Information: FPRO_10297-t41_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRO_10297-t41_1-p1
• CAZy Family: GH3
• CAZyme Description: related to 6-hydroxy-d-nicotine oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
495	FJOF01000005|CGC8	54720.05	8.5795

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=FJOF01000005:252517-254238(+)

Full Sequence      

MKTSASVLAWASALLAASPAVAMETCCASLEAKGLKHVYYPNSNGYKTRTESYFSVSSQL
EPYCIVQPESAKDVSTIIKTLTSDTKCNFAIRSGGHTVWAANNINDGVTIDMGLMNKTTY
VKNTKVAQIQAGSIWRDVYGALEPYGATAAGGRTSTVGVAGFLTGGGNTFYTARRGFGCD
QVVNFEVVLGDGRIVNANKDNNADLWKALKGGSANFGIVTRFDVQAFDAPLLWGGLVTYS
AEETTDAHVQAYKDWTDNIVNYQDGSVIPFWSYTPQAGKIGITVSYEDTTGAVAPKALDE
FWKIPYETSNLRKDTHRNMTIELELVAGYRNVWFAITFKNKLGLYKKALELHKQFVSDWK
AQSPDGDFICHAIFQAIPTIFSKHSLERGGNVVGLDREKDNAVMFQVQLMINGVEQEKIA
RERMVRFRKTMKQYSIDQGAAVDWEYLNYADFTQDPLSTYGPKNVEFIRKVAKKYDPKGV
FQTRLPGGFKISKVA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	59	258	1e-49	0.4344978165938865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.57e-20	62	198	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	1.80e-20	62	230	32	207	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	3.69e-09	59	221	62	233	cytokinin dehydrogenase
273751	FAD_lactone_ox	1.86e-06	67	226	20	186	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.
178402	PLN02805	2.73e-05	62	220	134	298	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK90596.1|AA7	2.49e-16	62	255	20	215
QRW22693.1|AA7	9.41e-16	38	266	37	267
UJO18775.1|AA7	1.03e-15	25	228	37	240
UJO20529.1|AA7	4.33e-15	18	259	43	288
ADI58761.1|AA7|1.1.3.-	6.70e-15	54	260	29	238

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYE_A	9.38e-17	90	264	72	242	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	2.22e-16	90	264	72	242	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]
6FYF_A	3.94e-16	90	264	72	242	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]
6FYG_A	3.94e-16	90	264	72	242	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]
3HSU_A	6.03e-16	54	260	35	244	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|C8VPE5|SDCF_EMENI	9.13e-102	20	493	2	478	FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	3.48e-97	22	494	40	516	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	2.11e-59	39	492	55	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|D4B1P2|A2372_ARTBC	1.20e-50	27	491	29	499	Uncharacterized FAD-linked oxidoreductase ARB_02372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02372 PE=1 SV=1
sp|B6H064|PRX3_PENRW	3.86e-47	40	490	45	506	FAD-dependent monooxygenase prx3 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=prx3 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000289	0.999682	CS pos: 22-23. Pr: 0.9704

TMHMM  Annotations     

There is no transmembrane helices in FPRO_10297-t41_1-p1.