CAZyme Information: FOMG_17694-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOMG_17694-t38_1-p1
• CAZy Family: GT32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
523		56636.36	5.8941

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum26406	20033	1089452	372	19661

• Gene Location: location=JH659389.1:27989-29684(+)

Full Sequence      

MVAKHLVFVVATLGTTLTAVSQSNEVTTGFKGCDALLDSGLNDIVVFPGSSAYNTSMSTY
YSSENRRVQPWCIVQPRSAQQVSTVVQALGNVSGAGHWGVAVRSGGHGYTGSNAIRYGVI
IDLTFLNSTELVQASHDNEASHWNGTSVISTSIARIHPAAKWGNIISYLEQYNLSVTGGR
SGDVGAAGLLLAGGISYHSQLWGMSCDNVINYEVVLANGSIIEANRHHNKDLFRALKGGG
NNFGIVTRFDMRTFTLPPDGVYGGLMVPTWDSVDTVKHQFVDYVHSIGMGSHDHEFVVWR
SNGTDHNMMVMTVSTDGNKASPNFLPFDNISTDYDFRALQPLSNLAASTSDTGGSYDMAF
VLTLQATMDIMDKCEEVFLSLAKDVKQAQIPLSITAVFQPLPKHLASASSDGNVLGLKQN
LPDSSIIFDIGGTLEDSAIEYEGVAYSKLAKAVEELRLFSAARERHSSYVYMNYANPEQD
TIGSYGNDNVEFLKYVAAKYDAHGFFQYRVSGGAKLSRAGYHD

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	67	279	1.2e-47	0.4192139737991266

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.58e-16	49	273	7	223	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	9.25e-12	70	225	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	2.54e-06	70	269	134	320	D-lactate dehydrogenase [cytochrome]
215242	PLN02441	0.005	66	248	61	233	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAI44126.1|AA7|CBM18	1.14e-18	39	257	246	444
QBZ61916.1|AA7|CBM18	1.14e-18	39	257	246	444
QRD93627.1|AA7	1.05e-16	42	254	21	214
UDD63515.1|AA7	1.05e-16	42	254	21	214
ANF89368.1|AA7	1.53e-16	35	277	25	251

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5K8E_A	5.29e-18	35	277	25	251	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]
6FYD_A	6.08e-18	45	258	22	213	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	1.08e-17	45	258	22	213	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	1.08e-17	45	258	22	213	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]
6FYE_A	1.92e-17	45	258	22	213	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|C8VPE5|SDCF_EMENI	7.05e-56	33	519	8	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|M2T7Z1|TPCD_COCH5	3.09e-55	19	517	16	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	4.75e-53	33	518	45	515	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|A0A2G5ICA0|CTB5_CERBT	5.21e-39	33	516	45	524	FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1
sp|W6Q5R7|PRX3_PENRF	1.50e-38	43	516	41	507	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	0.999724	CS pos: 21-22. Pr: 0.9239

TMHMM  Annotations     

There is no transmembrane helices in FOMG_17694-t38_1-p1.