CAZyme Information: EEU34981.1

Basic Information

• Species: Fusarium vanettenii
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
• CAZyme ID: EEU34981.1
• CAZy Family: AA6
• CAZyme Description: FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:C7ZLZ3]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
492	GG698948|CGC3	53547.50	7.7643

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fvanettenii77134	15708	660122	0	15708

• Gene Location: location=GG698948:95833-97511(-)

Full Sequence      

MLPSSSLIELILLVATATEGRATSLAPLARQDLRSCLSSAVGGDAARAQFQDEPDFISKD
VNYHNLNLQCEPFAVPYPKTKDEISEVLACAVKHKRKVQPRSGGRDFINQCLGGADDAIV
VDLKHFNHLSVDKTTGIATVGPGNLLKDLVEGLNNAGRFMPHGSSPTVGIGGLIAVGGIG
YTSRENGLSIDVMQEVEVILANGTVTRATKMTNSDLFWSMSGAGASFGIATEFKFQTKPM
LKELTTFSYNYSTTDKALLARAMKAFNKLASEKSTSRKVSRSGNLAKNSFYVSGVFLGHK
KDFDALSLDKHFPFGAEKTVRGCISWIDYMNGLFRGASNVPGQAYSYAKDLAVGGRNVSS
DSAVERFVDHVQAADSGAVYWSYLFDWYGGAVNDVDTGATPFPHRNLRYFMSTYATTTQE
TSEKTMNFIDDGILALQNNKPANYLHYAGVPNLRLSSKAQEKCFIIHHHVTRDSFSLPFS
SISWPSLFGNDL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	63	282	2.1e-64	0.4759825327510917

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.45e-33	72	209	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	4.71e-31	72	260	32	226	FAD/FMN-containing dehydrogenase [Energy production and conversion].
273750	pln_FAD_oxido	1.02e-08	70	264	30	232	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.
178402	PLN02805	4.23e-07	72	257	134	324	D-lactate dehydrogenase [cytochrome]
273751	FAD_lactone_ox	3.64e-06	70	217	13	158	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
UPK90289.1|AA7	2.62e-83	112	462	9	338
CCA70426.1|AA7	1.37e-79	13	460	28	486
CAE7010772.1|AA7	1.06e-77	33	444	13	428
AHG26149.1|AA7	1.57e-77	28	461	1	438
QRD86662.1|AA7	2.38e-77	14	462	5	452

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO4_A	4.12e-40	28	425	9	407	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	2.04e-39	28	425	9	407	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
3RJ8_A	3.30e-38	59	448	24	429	Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]
6Y0R_AAA	4.38e-38	23	423	17	420	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
3HSU_A	6.38e-34	45	448	15	436	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B6HNK6|SORD_PENRW	8.93e-68	35	457	9	433	FAD-linked oxidoreductase sorD OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=sorD PE=3 SV=1
sp|I1SB12|MNCO_MICNN	1.25e-37	22	448	14	451	Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2
sp|I1S2K2|CHITO_GIBZE	2.25e-37	23	423	17	420	Chitooligosaccharide oxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=chitO PE=1 SV=1
sp|Q6PW77|GOOX_SARSR	1.23e-33	30	448	25	455	Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1
sp|G2QG48|XYLO_MYCTT	2.71e-32	60	406	49	403	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 SP

Other	SP_Sec_SPI	CS Position
0.000284	0.999692	CS pos: 22-23. Pr: 0.8942

TMHMM  Annotations     

There is no transmembrane helices in EEU34981.1.