CAZyme Information: FVEG_10149-t26_1-p1

Basic Information

• Species: Fusarium verticillioides
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium verticillioides
• CAZyme ID: FVEG_10149-t26_1-p1
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
532		56909.34	7.2993

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=CM000586.1:2299557-2301155(+)

Full Sequence      

MQTSSMQNLRATLLRGLLVLAAPAVASCHCSTAPQACSILASALPAEAFVAPNSTGYETV
QSSYWSETAGDLSPACITRPKNTEQVASIVKILSSCGSDVQFAVKSGGHGSWPGWSSTDC
GVLISLDLIDGVQNVADSGYAVVGSGARWVDVYKKLEPHGVTVIGGRFASIGVGGLVVGG
GISYFTGLHGMACDNVLDYEVVLAGGTVANVSQTSKPDLFRALKGGGNQFGIVTRFSLKT
YKQTTQVWAGILTFSIDKASQVFNAMQTFIARYDPLSHIYLSMGGGSNPQLSFINVYIFY
NASSPPAGGANPFAAFYAAEPIADTTSTQNYSTLIALNNNGNTPQNRWLIGGHTFPNLLA
PYGADMYLKQWQAFRDMANSTAAGDQNLLFSMALVPVPAVAMRAGENVTGVQNVLGLEPD
AGDAVWIDYTLAWLDTKDDRKMFGFVERISNAGDRLATSFAPGVASTNAIPGAVTAKEAE
FYRTNPRYMNYALLDQPVQSSYGKKNERFLKRVQKRYDPNGLWRKNGGFLWD

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	68	526	3.1e-58	0.9737991266375546

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	4.61e-19	74	212	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	7.45e-18	74	267	32	231	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	3.84e-13	74	235	65	233	cytokinin dehydrogenase
178402	PLN02805	1.38e-06	74	242	134	306	D-lactate dehydrogenase [cytochrome]
273751	FAD_lactone_ox	2.38e-04	60	255	2	207	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
QRD93627.1|AA7	3.20e-21	74	264	48	237
QMW46638.1|AA7	3.20e-21	74	264	48	237
UDD63515.1|AA7	3.20e-21	74	264	48	237
QPH04356.1|AA7	4.79e-21	74	284	121	332
AAS79317.1|AA7|1.1.3.-	1.59e-20	71	248	59	243

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.01e-22	52	526	25	456	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]
6FYE_A	1.81e-22	52	526	25	456	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYF_A	1.81e-22	52	526	25	456	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	1.81e-22	52	526	25	456	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]
2BVF_A	2.34e-22	74	283	39	245	Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVF_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVG_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVH_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|M2T7Z1|TPCD_COCH5	1.19e-63	27	523	29	507	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|D4B1P2|A2372_ARTBC	2.49e-58	52	439	42	419	Uncharacterized FAD-linked oxidoreductase ARB_02372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02372 PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	2.15e-55	28	529	36	511	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|A0A2P1DP98|MACF_PENTR	6.90e-49	37	525	56	507	FAD-dependent monooxygenase macF OS=Penicillium terrestre OX=374132 GN=macF PE=3 SV=1
sp|C8VPE5|SDCF_EMENI	8.63e-49	52	532	23	477	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000634	0.999339	CS pos: 27-28. Pr: 0.9415

TMHMM  Annotations     

There is no transmembrane helices in FVEG_10149-t26_1-p1.