CAZyme Information: FOMG_17576-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOMG_17576-t38_1-p1
• CAZy Family: GT31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
504	KI980356.1|CGC1	55614.85	5.6363

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=KI980356.1:43120-44747(+)

Full Sequence      

MKFESLLVAVSVGRGFAQASGTATCVIACDAVAKLYPDRIITPSSTAFRSSQLEYWNAPQ
RNTAPACFFQPKSAEQVQAAIKIVIQAKCPFSIKGGGHSSNFGGSSIEGGFQFDLVDIAH
HDIVNEGRSVNIGPGIRWGPLFSFLEEHGLTVAGGRDSGVGVPGFLFGGGISYFAAQRGW
GVDQLTSTDLVLANGTLITVDSTSYPDLHKALQGGGAQNFGIVTSLTLNTFESGGMWGGI
KVTTTDNFENVFKAYDSFAKDVPKDGKAHLFMDFARVNGTLIIAQYMYYSEPVKDPKIFD
NFRPIPAVIDTLRIANHSDFAKEMEQITDTRSKRNLYWTRTFNFDVELLKSIYGLWVNIS
EAYADRLTAALDAQLIYPKMRKGSSAGRLFGLDDSEDVLQLIVISIIWENEADDEEAIKI
VRELDADIDRLVKLRGTHRDFKYMNYGHMEQDIIAGYGQENQAFLKRIALQYDPDSVFQK
LRRGGFKFGKVAHDTPDLGNHDEL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	56	280	4.9e-48	0.4890829694323144

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	8.78e-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	2.25e-22	56	478	23	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
273751	FAD_lactone_ox	1.11e-07	65	257	15	202	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	4.56e-05	71	228	140	302	D-lactate dehydrogenase [cytochrome]
215242	PLN02441	3.61e-04	64	224	64	232	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANF89368.1|AA7	1.37e-18	65	233	61	230
AEO58513.1|AA7|1.1.3.-	1.37e-18	65	233	61	230
QGA17347.1|AA7	9.30e-18	39	283	23	269
EGX49222.1|AA7|CBM1	3.31e-17	65	233	164	333
UNI23960.1|AA7	2.22e-16	43	235	27	219

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO5_A	5.63e-21	39	273	24	260	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6EO4_A	5.63e-21	39	273	24	260	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
5K8E_A	4.73e-20	65	233	61	230	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]
3HSU_A	4.84e-17	65	247	43	225	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
1ZR6_A	6.44e-17	65	247	43	225	The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|M2T7Z1|TPCD_COCH5	2.04e-72	55	487	69	516	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	1.25e-64	27	491	7	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|A0A0U5GQ05|DRTC_ASPCI	1.90e-62	48	491	66	516	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|B6H064|PRX3_PENRW	1.82e-50	28	488	31	507	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	2.46e-48	28	487	31	506	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
0.818039	0.181968

TMHMM  Annotations     

There is no transmembrane helices in FOMG_17576-t38_1-p1.