CAZyme Information: SPSK_06269-t39_1-p1

Basic Information

• Species: Sporothrix schenckii
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii
• CAZyme ID: SPSK_06269-t39_1-p1
• CAZy Family: GH32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
483	AXCR01000001|CGC5	51134.10	5.6297

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sschenckii1099-18	10434	1397361	141	10293

• Gene Location: location=AXCR01000001:3116736-3118187(-)

Full Sequence      

MSSSQLPPLSLTCEVKFPSKDDNLHDHVVRWSDIHVSVPAVVVIPESESDVVAAIVYAKD
NSLRVVVAGGGHAPFIPVTAKTLYLDLRRFKSIVLDEGASTVTIGGGVLTGELLTYLLER
GFYATLPNSSAVGVVGAVLGVGNGPFNSLHGFMADNVESVRIVTLPKEGAAASRNISHSS
TGADERSLFAAVCGAGHGLGVIVSMTLRAYKVADLRLEGGDQVWNRRGVFPAPAIRDAAR
AFVSLLPLTGPANATLLIARSPPNMPRPGSPIALLVAAHFGPSAEAEASPAAKILLGEDF
AAKAAVAVTEGVPLAKLNASTEPFNAVGGSKILSGTYLHSINEDVIVSLFERFVGFTNER
PDLWNTYIAIPTWNTTKSLQLGASPERKDNFHVARDRNVLVLSAVWSKTGGADIESESST
YSAEIQEIAGREESGPLIGFANNLAFPAKLADYYPADKVDELARVKTQWDPNGLFWSPSM
GVE

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	29	477	4.9e-37	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.21e-18	38	477	31	452	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	4.65e-17	39	164	1	130	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.
273751	FAD_lactone_ox	1.72e-07	31	208	7	177	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.
223882	MurB	1.95e-04	30	129	11	117	UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis].
178402	PLN02805	3.09e-04	3	212	90	307	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD00400.1|AA7	1.48e-12	20	478	25	469
QRC92907.1|AA7	3.16e-09	39	217	63	237
UPK90596.1|AA7	5.02e-09	39	483	20	442
UQC82098.1|AA7	1.24e-07	17	211	37	225
UIZ28076.1|AA7	1.73e-07	39	217	97	270

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	6.03e-20	1	246	2	231	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]
6FYD_A	3.43e-12	1	475	1	453	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	4.55e-12	1	475	1	453	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	6.05e-12	1	475	1	453	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYF_A	8.03e-12	1	475	1	453	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|G4N285|OXR1_MAGO7	8.58e-22	30	475	69	496	FAD-linked oxidoreductase OXR1 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR1 PE=1 SV=1
sp|Q7SHH8|SRDI_NEUCR	8.65e-21	7	475	43	489	FAD-linked oxidoreductase srdI OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=srdI PE=2 SV=1
sp|P08159|HDNO_PAENI	9.55e-20	1	246	1	230	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2
sp|G3XMC1|AZAG_ASPNA	4.59e-16	7	211	29	227	FAD-linked oxidoreductase azaG OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaG PE=2 SV=1
sp|G3XMD0|AZAL_ASPNA	4.67e-16	9	244	31	255	FAD-linked oxidoreductase azaL OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaL PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000046	0.000000

TMHMM  Annotations     

There is no transmembrane helices in SPSK_06269-t39_1-p1.