CAZyme Information: FPRO_15102-t41_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRO_15102-t41_1-p1
• CAZy Family: GT22
• CAZyme Description: related to 6-hydroxy-D-nicotine oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
593		66359.87	7.2324

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=FJOF01000009:1809515-1811296(-)

Full Sequence      

MTSAQVNGFIGMQYSREGSDYEKGDYKFFNEQYATSSYIDVLDPSGKPSHDLNPALILRP
KDDEGVKAVIHHAVKNKVGIAIKSGGHQYSGASSCGGQNVQLDLSNTYKDLKIVDVSILD
KTKTTVAHDRVLVFAGVSNQLQDFLAYLTSHKLFVPTGQCAYVCLGGHGQTGGYGQLGRS
FGLLGDYIVDIRLIDHQGEVKHVNQGQDAELFNAIRGGSPGNFGVVTHYTISALKAKSYM
GIENTITTPNNPKPEKFQGPHGIKAAWIYSEKVLRNLLNIVAKMSDEGTAPRGFDLCVNV
LSTDFDITKLFPALKTDEEWKGVQDVISKLPGPVKDLLNGKLPPLIVLYAQWCPVGDQQK
YDASVDAWFQQFRGLKYFRIQFDEISADMSDMVGHWLFPKRREFPRPYVKRTYATNSKTL
GKDGWVDTLVERLSKICSPYEKLDDANQKPVDNPLYDNCKISAQIQCFGGDNSMFYNNRN
NGAAYSWRDSTVLQTVDCWYLNRTDPNYKKSLELANEWQAKNDSVMIGANSCFSKTDRRV
LWGSWGDWDMAKPEVWKTYYEDEAKYQSIGKVRAAADPKGTFTANPFAVERQE

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	51	249	8.7e-44	0.39737991266375544

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.24e-09	54	231	32	201	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	6.70e-08	54	204	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.
178402	PLN02805	0.006	46	239	121	310	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK91582.1|GH31	1.85e-118	17	590	6	517
UKZ49297.1|GH31	2.26e-117	17	590	8	520
UKZ75824.1|GH31	1.98e-115	17	590	8	520
QYS96687.1|GH31	2.79e-115	17	590	8	520
RDX44700.1|AA7|1.1.3.-	6.33e-14	51	230	66	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7E2V_A	4.74e-17	30	257	59	274	Chain A, MaDA-3 [Morus alba],7E2V_B Chain B, MaDA-3 [Morus alba]
6FYD_A	2.37e-14	51	229	42	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]
6JQH_A	2.82e-14	30	257	30	245	Chain A, MaDA [Morus alba],6JQH_B Chain B, MaDA [Morus alba]
6FYF_A	4.18e-14	51	229	42	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]
6FYB_A	5.55e-14	51	229	42	204	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A3RXB7|HEXNO_RALSU	2.05e-15	48	234	24	201	N-acetyl-D-hexosamine oxidase OS=Ralstonia solanacearum (strain UW551) OX=342110 GN=RRSL_02030 PE=1 SV=1
sp|A0A140JWT7|PTMO_PENSI	2.84e-15	54	231	36	198	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	6.68e-15	54	231	36	198	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|Q9SVG4|RETOL_ARATH	7.52e-15	49	242	82	263	Berberine bridge enzyme-like 19 OS=Arabidopsis thaliana OX=3702 GN=At4g20830 PE=1 SV=2
sp|Q93ZA3|BBE13_ARATH	1.21e-14	25	231	50	251	Berberine bridge enzyme-like 13 OS=Arabidopsis thaliana OX=3702 GN=At1g30760 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000063	0.000002

TMHMM  Annotations     

There is no transmembrane helices in FPRO_15102-t41_1-p1.