CAZyme Information: FOC1_g10002247-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOC1_g10002247-t38_1-p1
• CAZy Family: AA7
• CAZyme Description: 6-hydroxy-D-nicotine oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
584	KB730290|CGC2	65358.61	7.1844

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporumrace1	15626	1229664	188	15438

• Gene Location: location=KB730290:47325-49079(+)

Full Sequence      

MATAQVNNFIGMQYAREGNEYEKEDYNFFNQQYATSSYIDVADHNLDPALILKPKDDNDV
KSAINYAVEHKVGIAIKSGGHQYSGACSCSGKNVQLDVSNAYKDLKIISNPTIPVPDDRV
LVFAGVGNQLQDFLAYLASHGLFAPTGQCAYVCLGGHGQTGGYGQLGRSFGLLGDYITEI
RMIDHSGKVQIINKDQNAELFYAIRGGSPGNFGVITHYTIMVFKAKSYMGIENTIKTPKG
PVKFQGPRGVKAFWLYNENTLKSLLGFVAAMSDAGNAPRGRDLCVNVLSTDFDITKLFPS
FKNDEVWKGLQDTVFRFFPDNIRALLAGKLPPVIVLYAQWCPVGDQQKYDESTDAWFQQF
RNLDNFKHGCVHFDEFPADMANMTGHWVFPQRREFPRPYVKRTYATNSKTLGKDGWVNTL
VGRLGKICDPYEKLDDANERPVPNPLYDNCKLSAQIQCFGGENSMFYKNGDGSSAYSWRD
STVLQTVDCWYLNINDPNHKMSQNLANQWQNENDGVMIGAKSCFSKTDRRVLWGSWGSWV
MASPDVWKTYYEDEAKYQRLGKARAAADPNGTFTANPFAVARQS

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	47	229	1e-46	0.37554585152838427

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	2.21e-11	39	220	23	201	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	1.76e-10	48	193	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	0.007	48	228	134	310	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK91582.1|GH31	1.21e-113	26	580	17	516
UKZ49297.1|GH31	1.47e-112	30	580	23	519
QYS96687.1|GH31	4.11e-112	26	580	19	519
UKZ75824.1|GH31	1.28e-110	30	580	23	519
RDX44700.1|AA7|1.1.3.-	2.89e-17	32	280	53	290

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	5.57e-15	48	253	45	233	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	9.84e-15	48	253	45	233	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]
7E2V_A	1.28e-14	48	236	83	264	Chain A, MaDA-3 [Morus alba],7E2V_B Chain B, MaDA-3 [Morus alba]
6FYG_A	1.31e-14	48	253	45	233	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]
6FYB_A	1.31e-14	48	253	45	233	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|O06997|YVDP_BACSU	6.51e-18	38	235	28	211	Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1
sp|Q9SVG4|RETOL_ARATH	1.07e-16	30	229	76	270	Berberine bridge enzyme-like 19 OS=Arabidopsis thaliana OX=3702 GN=At4g20830 PE=1 SV=2
sp|Q54H55|Y8969_DICDI	2.12e-16	48	230	48	218	FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
sp|Q9SA89|BBE12_ARATH	3.94e-16	48	358	77	341	Berberine bridge enzyme-like 12 OS=Arabidopsis thaliana OX=3702 GN=At1g30740 PE=2 SV=1
sp|Q9SVG3|BBE21_ARATH	4.02e-16	48	229	86	269	Berberine bridge enzyme-like 21 OS=Arabidopsis thaliana OX=3702 GN=At4g20840 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000052	0.000001

TMHMM  Annotations     

There is no transmembrane helices in FOC1_g10002247-t38_1-p1.