CAZyme Information: FVEG_10867-t26_1-p1

Basic Information

• Species: Fusarium verticillioides
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium verticillioides
• CAZyme ID: FVEG_10867-t26_1-p1
• CAZy Family: GH43|CBM91
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
540	CM000588.1|CGC12	59068.78	5.0912

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fverticillioides7600	16240	334819	371	15869

• Gene Location: location=CM000588.1:972722-974496(+)

Full Sequence      

MRCISLAVAAFLVVKSSATDSLLETKDFNITQALLDQGVDVSELPVSVDGPKRSDTGCAA
ACASLKILYGDAAVETRNEEDFRDFTASYWSSNQAEVNPYCIFIPQRPSHVSVTVLLARL
AQCPFAAKSGGHAAFAGASSVEGGITISFANLKDVSLSKDKNTASIEPGNTWGPVYEQLA
KSDVSVIGGRLYNIGVGGLTTGGGISFFSNIYGWACDNVQSYEVVLANGIIVEASAKSYP
DLYWALRGGGNNFGLVVKFNLKTIPLPKSEMWGGSRIYTEDRFSEVTDALFNILKNSEND
PKAGLYVPWVYYQGNKFSMPTMYYAEPDAGNATIWKDFNKIEAVSDTTQNRVLAGWGKEL
MSDSPPGLREVYYVITTKLDHGILEYTRDYFYKTVLTVANISGIIPALVVQGITTPQLKQ
MQKNGGNALGIDPEDGPLLILQLSVMWTNKSDDDAIYSWISDIFEVVTKEAKARGVNNDY
VYMNYASQYQDVIASYGSGNKAKLKSIAKKYDPQQVFQKLQPGYFKLDRAPIPNSGYFSH

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	89	296	4.5e-58	0.4497816593886463

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	2.65e-18	99	235	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	9.90e-12	99	269	32	209	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA09402.1|AA7|CBM18	3.42e-22	76	517	48	512
ANF89368.1|AA7	2.20e-20	74	267	38	231
AEO58513.1|AA7|1.1.3.-	2.20e-20	74	267	38	231
QSZ37541.1|AA7|CBM18	6.30e-20	76	537	45	527
CCD53507.1|AA7|CBM18	8.10e-20	76	269	48	249

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5K8E_A	7.59e-22	74	267	38	231	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]
3RJ8_A	2.90e-19	86	268	19	209	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]
6FYD_A	1.17e-18	111	259	57	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]
6FYF_A	2.08e-18	111	259	57	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]
6FYG_A	2.08e-18	111	259	57	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|M2T7Z1|TPCD_COCH5	1.94e-82	89	528	69	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	6.94e-75	59	532	42	518	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|C8VPE5|SDCF_EMENI	1.18e-62	62	530	9	479	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|A0A023I4D6|PRX3_PENRO	3.52e-62	59	531	29	511	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|W6Q5R7|PRX3_PENRF	3.52e-62	59	531	29	511	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000241	0.999730	CS pos: 18-19. Pr: 0.9773

TMHMM  Annotations     

There is no transmembrane helices in FVEG_10867-t26_1-p1.