CAZyme Information: ASPVEDRAFT_144681-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_144681-t33_1-p1
• CAZy Family: CE16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
506		54411.75	4.4401

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AversicolorCBS583.65	13364	1036611	142	13222

• Gene Location: location=KV878140:204849-206369(+)

Full Sequence      

MIVPTLLLLTAQALADDYRPLFHFVPEKNWMNEPNGLIKIDSVWHLFYQHNPTENVWGNL
NWGHATSTDLVHWTHEPIAITSEDGVEAFTGTSYYDAENTSGLGTTQSPPYLAWYTGYFP
SNGTQDQRLAYSVDGGVTYTKFAGNPIISAAQEAPHDTTGGLETRDPKVLFHEASGKWVM
ILAHGGQDKVTFWTSTDAKRWTWVSDLGTAQVPGLPANITGWEVPDLFQLPIEGTDETTW
VLILTPAKGSPAGGNGVFALTGSFDGESFKPDPVESGNLWLDYGRDFDGAMSWENVPGSD
GRRILAGISNSYGASPPTNTWKGMLSFPRTLALQQTGSARSFIQWPVSELLDIGSPLTTI
QNKTIAPGQTLLSSVGGTALDIELAFTPQKDAILSLAVRKAGSQQTVIQYKQSTATLSVD
RTASGDTTYDAAAGGVHNASLQPDSSGLVHIRTLVDTCSVEVFGGKGKVVISDLIFPDDT
ADGLALQVTGGSVMLQSVVVREVSLE

Enzyme Prediction     

EC	3.2.1.7:10

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	23	346	3.3e-77	0.9965870307167235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350134	GH32_Inu-like	1.23e-123	28	333	1	289	glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
214757	Glyco_32	3.14e-118	23	467	1	437	Glycosyl hydrolases family 32.
224536	SacC	3.14e-100	16	497	26	479	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
395193	Glyco_hydro_32N	4.92e-97	23	346	1	308	Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.
350110	GH32_FFase	3.08e-74	29	333	1	281	Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS23485.1|GH32	0.0	41	506	41	506
AFT91384.1|GH32	4.40e-293	1	497	1	497
BAA12321.1|GH32|3.2.1.7	1.48e-267	13	505	23	515
BAA12320.1|GH32|3.2.1.7	1.48e-267	13	505	23	515
BAA33797.1|GH32|3.2.1.7	2.53e-266	7	506	17	516

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3RWK_X	1.44e-266	7	506	17	516	First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum],3SC7_X First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum]
1Y4W_A	2.40e-93	18	492	7	502	Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P21 [Aspergillus awamori],1Y9G_A Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose [Aspergillus awamori],1Y9M_A Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 [Aspergillus awamori]
3KF3_A	5.77e-62	19	334	10	312	Chain A, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	6.16e-62	19	334	13	315	Chain A, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3U14_A	2.74e-61	19	334	36	338	Chain A, Fructofuranosidase [Schwanniomyces occidentalis],3U14_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K0E681|ECDF_ASPRU	7.82e-294	1	497	1	497	Putative glycosyl hydrolase ecdF OS=Aspergillus rugulosus OX=41736 GN=ecdF PE=3 SV=1
sp|O74641|INUA_ASPNG	4.50e-267	7	506	17	516	Extracellular endo-inulinase inuA OS=Aspergillus niger OX=5061 GN=inuA PE=1 SV=1
sp|O94220|INU2_ASPFI	7.41e-266	7	506	17	516	Extracellular endo-inulinase inu2 OS=Aspergillus ficuum OX=5058 GN=inu2 PE=1 SV=1
sp|A5ABL2|INUA_ASPNC	1.49e-265	7	506	17	516	Extracellular endo-inulinase inuA OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuA PE=1 SV=1
sp|O74642|INUB_ASPNG	4.96e-264	7	506	17	516	Extracellular endo-inulinase inuB OS=Aspergillus niger OX=5061 GN=inuB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000271	0.999751	CS pos: 15-16. Pr: 0.9737

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_144681-t33_1-p1.