CAZyme Information: FOYG_13962-t42_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOYG_13962-t42_1-p1
• CAZy Family: GH76
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
504	JH717847.1|CGC5	55287.45	6.0589

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumNRRL32931	17642	660029	362	17280

• Gene Location: location=JH717847.1:2259698-2261320(+)

Full Sequence      

MKFESLLAAASVGRGFAQASVTSTCVKACDAVAKLYPDQVITSSSSAFKHAQLEYWNGPQ
RNTAPACFFQPTSANQVQAAIKEVTKLQCPFSIKGNGHSSNFGGSSIEGGFQFDLVNIAH
HDIVSDGRSVKIGPGNRWGPLFSFLEEHGLTVAGGRDSGVGVSGFTFGGGISYLAAQRGW
GADQLISADLVLANGTLITVDSTSHPDLHKALRGGGAQNFGIVTSMTLNVFQFGGMWGGI
KVTTADKFEQVFNAYDKFAKKVPEDGKAHMFMDFARVNGTLIVAQYMCYAEPVKDPMIFD
DFRPIPAVMDTLRLANHSEFAKEMEQITDTRGKRNLYWTRTFGFDIELLKSIYGLWVKIS
DSYADRLTAALDAQLIYPKMRKDSSAGSLFGLDDSDDVLQLIVISIIWEDEADDEEAVKI
VRELDAEIDILVKVRGKHREFKYMNYGHNEQDIVTGYGQKSKAFLKRVASQYDPDGVFQK
LRLGGFKIDNNADNTLGHGSHDEL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	55	272	1.3e-51	0.4737991266375546

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	9.69e-23	65	201	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	2.65e-20	38	478	9	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	1.33e-06	20	224	22	232	cytokinin dehydrogenase
273751	FAD_lactone_ox	5.18e-06	65	230	15	178	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.
178402	PLN02805	6.02e-04	55	228	118	302	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJO20529.1|AA7	1.57e-17	65	228	90	253
EGX49222.1|AA7|CBM1	3.31e-17	65	231	164	331
CDR44461.1|AA7	3.56e-17	41	356	48	376
ANF89368.1|AA7	1.04e-16	65	231	61	228
AEO58513.1|AA7|1.1.3.-	1.04e-16	65	231	61	228

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO5_A	5.78e-20	45	278	30	265	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6EO4_A	5.78e-20	45	278	30	265	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
5K8E_A	3.59e-18	65	231	61	228	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	5.51e-18	39	265	21	243	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]
6FYG_A	9.82e-18	39	265	21	243	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	8.33e-71	10	488	15	517	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|C8VPE5|SDCF_EMENI	1.92e-62	19	489	2	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
sp|A0A0U5GQ05|DRTC_ASPCI	2.97e-58	48	488	58	513	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|B6H064|PRX3_PENRW	3.51e-50	19	490	22	509	FAD-dependent monooxygenase prx3 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=prx3 PE=2 SV=1
sp|A0A023I4D6|PRX3_PENRO	1.30e-49	19	490	22	509	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.898615	0.101426

TMHMM  Annotations     

There is no transmembrane helices in FOYG_13962-t42_1-p1.