CAZyme Information: KZZ95574.1

Basic Information

• Species: Ascosphaera apis
• Lineage: Ascomycota; Eurotiomycetes; ; Ascosphaeraceae; Ascosphaera; Ascosphaera apis
• CAZyme ID: KZZ95574.1
• CAZy Family: GT22
• CAZyme Description: Glyco_hydro_32N domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A168BPL1]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
515		58725.09	5.0446

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AapisARSEF7405	6442	392613	0	6442

• Gene Location: location=AZGZ01000004:20394-21941(+)

Full Sequence      

MSSTDSFKPSGLYRRQNPPSLYTSGDPQPILVGDTYHLLNLAGPADTFDINERVFCHWPH
YRSKDLVNWTLDKEPAFVPSTNPDDPDVGGVWAGCVITGPDGNMHVFYAGHSEAQEQPQC
VVHAVSDDPHGNKFTKLGVINISEKTKGNLLKTYEMKDFRDPFVFYNEEEKKWWMLVSAR
LNKGPKWTRGALALLTSEDFKTWDVEEEPLYAPNDVHVPECPELFKLGEKWYLIYARYIA
PEAGAAYLIADSPRGPFRHPPGGRYLDGRRWYAAKSCPKAGDDTKRIVFGWIGDRRKEDS
VWQWGGDTAAPRELWVGPDLSLRMGPCMEVLNGMFEQTPAYEVKSTVVKRLGGMEAKFLE
YPSTAAEKGQLVTFQAKPAPTTTGYGLLLRCDEDWSGYWLNFFPRRREGDITYHNITLTM
SPFTLDDWTGDHHDYTRREIDGTDFIRLEDVPIKDGETGRLVLLDDMIEFFIGGRALTFR
WGWSKYERDNADAPLGVFVQDGEVEFENFRVFKGY

Enzyme Prediction     

No EC number prediction in KZZ95574.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	26	316	2.1e-46	0.9249146757679181

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350109	GH32_EcAec43-like	1.57e-103	25	322	1	281	Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2). This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 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). GH32 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.
350110	GH32_FFase	7.82e-41	29	316	9	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.
350121	GH32-like	4.00e-39	33	275	18	270	Glycosyl hydrolase family 32 family protein. The GH32 family contains glycosyl hydrolase family GH32 proteins that 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). 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.
350093	GH_J	2.11e-38	25	315	1	292	Glycosyl hydrolase families 32 and 68, which form the clan GH-J. This glycosyl hydrolase family clan J (according to carbohydrate-active enzymes database (CAZY)) includes family 32 (GH32) and 68 (GH68). GH32 enzymes include invertase (EC 3.2.1.26) and other 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.-). The GH68 family consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10, also known as beta-D-fructofuranosyl transferase), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9). GH32 and GH68 family enzymes are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) and 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. 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	9.03e-37	26	474	11	436	Glycosyl hydrolases family 32.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UDD60227.1|GH32	1.97e-151	13	509	12	513
QMS79065.1|GH32	6.05e-143	12	511	9	510
QKD48851.1|GH32	4.42e-120	24	515	26	520
QGI85064.1|GH32	3.51e-119	24	515	26	520
QGI98716.1|GH32	3.51e-119	24	515	26	520

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6R3R_A	3.60e-14	84	413	96	427	First crystal structure of endo-levanase BT1760 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron]
6R3U_A	1.96e-13	84	413	96	427	Endo-levanase BT1760 mutant E221A from Bacteroides thetaiotaomicron complexed with levantetraose [Bacteroides thetaiotaomicron]
7VCO_A	2.49e-13	57	347	68	355	Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
1UYP_A	8.00e-11	58	331	46	299	The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_B The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_C The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_D The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_E The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_F The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B6DZD0|1FEH_TRIUA	1.38e-15	58	319	105	375	Fructan 1-exohydrolase OS=Triticum urartu OX=4572 GN=1-FEH PE=3 SV=1
sp|B6DZD1|1FEH_AEGSP	4.27e-15	58	319	103	373	Fructan 1-exohydrolase OS=Aegilops speltoides OX=4573 GN=1-FEH PE=3 SV=1
sp|Q84PN8|1FEH1_WHEAT	5.68e-15	58	316	105	372	Fructan 1-exohydrolase w1 OS=Triticum aestivum OX=4565 GN=1-FEHw1 PE=1 SV=1
sp|Q84LA1|1FEH2_WHEAT	9.98e-15	58	319	104	374	Fructan 1-exohydrolase w2 OS=Triticum aestivum OX=4565 GN=1-FEHw2 PE=1 SV=1
sp|B6DZD2|1FEH_AEGTA	1.32e-14	58	319	104	374	Fructan 1-exohydrolase OS=Aegilops tauschii OX=37682 GN=1-FEH PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000039	0.000002

TMHMM  Annotations     

There is no transmembrane helices in KZZ95574.1.