CAZyme Information: SAPIO_CDS7963-t41_1-p1

Basic Information

• Species: Scedosporium apiospermum
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum
• CAZyme ID: SAPIO_CDS7963-t41_1-p1
• CAZy Family: GH72
• CAZyme Description: Oxidoreductase, FAD-binding protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
488		55140.08	7.9700

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SapiospermumIHEM14462	10920	N/A	2544	8376

• Gene Location: location=JOWA01000114:58823-60433(-)

Full Sequence      

MSAARYTTTPNYSAKILVKGTPEYERCRTNNPSADTPARYPREIHVVKSAEDVSAALRRA
AELGVCVGVRSSGHIMNVPSLIDDGILIDTVELNRGLDYEPQSKVISFGPSVRVEEVAEG
LAKIGRFFPHGHAPTVGAGGFLLAGGQGWFVRGWGATNQTWIVKMEIVVPDGRIVIASPT
ENRDLWWAARGSGLAFFGVVTRFWCRTIATSLMWERTFKFEINTDNYETLMTWAIESGRS
TPKYGTDLNLTIDYPEKYDPRFTTDDVPPSRKLHMSLNLLCYTDTRREAVTLLSAYDKMP
KNVHDWLLEMKPVQRRTFEEVFARKRGFLGNSKNERWQINSIMNDPAVPLSRLLEGIKPA
MLELPTRTSSVFLCHCDIVPDEEDAALSLPQDLYISTITGWTDPSLEPAIYQPMRDRYRR
AFPVAVGMYITEIDVNNDDANTKVLSDTALAKFLQIREKWDPKGLFPNYKAIVRVHDKIN
KLQRKSLL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	34	239	1.4e-52	0.4410480349344978

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.69e-24	39	472	30	456	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	4.82e-16	47	178	7	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.
273750	pln_FAD_oxido	7.65e-04	22	225	25	223	plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.
215242	PLN02441	0.004	48	202	72	233	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANF89368.1|AA7	1.67e-17	13	237	33	247
AEO58513.1|AA7|1.1.3.-	1.67e-17	13	237	33	247
QUC19098.1|AA7	6.33e-17	40	207	40	214
CCA72155.1|AA7	8.46e-17	65	201	128	270
UNI23960.1|AA7	1.14e-16	49	472	56	469

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5K8E_A	5.77e-19	13	237	33	247	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]
6FYE_A	3.80e-17	39	203	43	204	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	9.03e-17	39	203	43	204	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]
2Y08_A	1.13e-16	41	207	59	232	Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y08_B Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y3R_A Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_B Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_C Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_D Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3S_A Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y3S_B Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y4G_A Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9],2Y4G_B Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9]
6FYF_A	2.14e-16	39	203	43	204	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A2I6PJ02|NODO_HYPPI	2.15e-28	23	464	21	438	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	4.76e-27	17	462	12	433	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	4.04e-26	17	236	12	228	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A0A0E3D8N0|JANO_PENJA	1.52e-24	23	252	18	241	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|O06997|YVDP_BACSU	9.61e-19	13	203	7	194	Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000047	0.000003

TMHMM  Annotations     

There is no transmembrane helices in SAPIO_CDS7963-t41_1-p1.