CAZyme Information: ASPBRDRAFT_515404-t33_1-p1

Basic Information

• Species: Aspergillus brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis
• CAZyme ID: ASPBRDRAFT_515404-t33_1-p1
• CAZy Family: GH92
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
516	KV878682|CGC7	55702.91	4.2432

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AbrasiliensisCBS101740	13263	767769	274	12989

• Gene Location: location=KV878682:1971228-1972778(+)

Full Sequence      

MLSPKVAYMVWMTCLGLSLPSQAQSNDYRPSYHFTPDQYWMNEPNGLIKIGSTWHLFFQH
NPTANVWGNICWGHATSTDLMHWAYKPTAIADEDGIEAFTGTAYSDPNNTSGLGTSTNPP
YLAWFTGYTTASQTQDQRLAFSVDDGATWTKFEGNPIISTSQEAPHDITGGLESRDPKVF
FHSPSGNWVMVLAHGGQDKLSFWTSADTINWTWQSDLKSTSIDGLASDITGWEVPDMFEL
PVDGTGETTWVVMMTPAQGSPATGNGVLALTGSFDGKAFTADPVDPSTMWLDNGRDFDGA
LSWVNVPASDGRRIIAAVMNSYGSNPPTTTWKGMLSFPRTLSLKKIGTQQRFVQQPITEL
DTISTSLQTLANQTITPGQTLLSSIQGTALDVRVAFYPDADSVLSLAVRKGASEQTVIRY
TQSNATLSVDRTQSGDISYDPAAGGVHTADLQEDATGLVSIRVLVDTCSIEVFGGQGEAV
ISDLIFPSDSSDGLALEVTGGNALLQSVDVRKVSLE

Enzyme Prediction     

EC	3.2.1.7:10

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	33	356	2.8e-74	0.9965870307167235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350134	GH32_Inu-like	3.94e-122	38	343	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	1.06e-120	33	477	1	437	Glycosyl hydrolases family 32.
395193	Glyco_hydro_32N	6.97e-101	33	356	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.
224536	SacC	7.04e-98	19	507	19	479	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
350110	GH32_FFase	1.31e-73	40	343	2	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
BAA33798.1|GH32|3.2.1.7	0.0	1	516	1	516
BAA33797.1|GH32|3.2.1.7	0.0	1	516	1	516
CAA07345.1|GH32|3.2.1.7	0.0	1	516	1	516
AAK43726.1|GH32|3.2.1.7	0.0	1	516	1	516
CAL00359.1|GH32	0.0	1	516	1	516

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3RWK_X	0.0	1	516	1	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	1.79e-92	28	514	7	514	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]
3KF5_A	1.23e-55	18	357	1	333	Chain A, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF3_A	2.24e-55	29	357	10	330	Chain A, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3U14_A	5.19e-55	18	357	24	356	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|A5ABL2|INUA_ASPNC	0.0	1	516	1	516	Extracellular endo-inulinase inuA OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuA PE=1 SV=1
sp|O94220|INU2_ASPFI	0.0	1	516	1	516	Extracellular endo-inulinase inu2 OS=Aspergillus ficuum OX=5058 GN=inu2 PE=1 SV=1
sp|O74642|INUB_ASPNG	0.0	1	516	1	516	Extracellular endo-inulinase inuB OS=Aspergillus niger OX=5061 GN=inuB PE=1 SV=1
sp|O74641|INUA_ASPNG	0.0	1	516	1	516	Extracellular endo-inulinase inuA OS=Aspergillus niger OX=5061 GN=inuA PE=1 SV=1
sp|K0E681|ECDF_ASPRU	1.22e-267	19	509	9	499	Putative glycosyl hydrolase ecdF OS=Aspergillus rugulosus OX=41736 GN=ecdF PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000221	0.999735	CS pos: 23-24. Pr: 0.9790

TMHMM  Annotations     

There is no transmembrane helices in ASPBRDRAFT_515404-t33_1-p1.