CAZyme Information: MGYG000004739_01797

Basic Information

• Species: Actinomyces sp000220835
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinomyces; Actinomyces sp000220835
• CAZyme ID: MGYG000004739_01797
• CAZy Family: GH68
• CAZyme Description: Levansucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
597		64672.19	4.3729

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004739	2692200	MAG	China	Asia

• Gene Location: Start: 6786; End: 8579 Strand: +

Full Sequence      

MTHPLFRARRRRLAAALAFALALGGAGTALAAEPDPAGQAPDAVAAPAIDPADPADPPDD
QAADAAGFQADNPGWPNATDHTQQAYPVDSDFTSTWTRADARQIQRVSDPNAPSGSSSLP
EQYTMPEISEGFPTTNDDVWVWDTWTLTDDAANQLSYNGWEIAFSLVADRHAGYTFDDRH
THARLGYFYRKAGTDESSEGGASASNGGWIYGGHVFPDGASGSIFEDQSFTSQTEWSGSA
RLMDGNKIRMFYTSVAFYQGSGGGYDAPAADTGKPYDPRIVQSEGRIYADDTGVWFTGFR
DQHQLLTPDGHYYQSRIQNPNVNFRDPFTFRDQNNPADSTDYMVFEGNSAYTREPELVDQ
VAAAGQNTTVASCTSKDMGYEAGDPKAESAQEVSDAGGRYQLANVGLARATNKAMTQWEY
LPPLLSGNCVNDQTERPQIYFKDGKYYLFTISHRETYAEGLMGPEGGYGFVGDGLRSDYR
PVNESTGIALGNPINLNVAPGRPYSPDWNQSPYTYQSYSHYVMPDGLVESFIDSIGGNHD
GSPVRGGSLAPTVKLLISGDTTTVDRSYGTNGLGGFGHIPANRSRDDGGDARPERLK

Enzyme Prediction     

EC	2.4.1.10	3.2.1.26

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH68	91	571	1.2e-146	0.9832134292565947

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam02435	Glyco_hydro_68	3.27e-139	91	566	1	410	Levansucrase/Invertase. This Pfam family consists of the glycosyl hydrolase 68 family, including several bacterial levansucrase enzymes, and invertase from zymomonas.
cd08997	GH68	1.66e-117	141	565	1	354	Glycosyl hydrolase family 68, includes levansucrase, beta-fructofuranosidase and inulosucrase. Glycosyl hydrolase family 68 (GH68) consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Levansucrase, also known as beta-D-fructofuranosyl transferase, catalyzes the transfer of the sucrose fructosyl moiety to a growing levan chain. Similarly, inulosucrase catalyzes long inulin-type of fructans, and beta-fructofuranosidases create fructooligosaccharides (FOS). However, in the absence of high fructan/sucrose ratio, some GH68 enzymes can also use fructan as donor substrate. GH68 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. 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. Biotechnological applications of these enzymes include use of inulin in inexpensive production of rich fructose syrups as well as use of FOS as health-promoting pre-biotics.
cd18609	GH32-like	7.44e-16	137	484	5	258	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.
cd08979	GH_J	1.06e-07	227	467	54	223	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.
cd08996	GH32_FFase	0.006	236	344	64	139	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
VEG27298.1	0.0	25	597	9	566
QQQ59919.1	0.0	1	597	3	636
QQC38808.1	0.0	62	597	95	636
QLF52964.1	0.0	62	597	95	636
AMD98227.1	0.0	62	597	95	636

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VSR_A	2.22e-199	76	583	8	488	Microbacteriumsaccharophilum K-1 beta-fructofuranosidase catalytic domain [Microbacterium saccharophilum],3VSS_A Microbacterium saccharophilum K-1 beta-fructofuranosidase catalytic domain complexed with fructose [Microbacterium saccharophilum]
3WPU_A	1.11e-198	76	583	8	488	Full-lengthbeta-fructofuranosidase from Microbacterium saccharophilum K-1 [Microbacterium saccharophilum],3WPU_B Full-length beta-fructofuranosidase from Microbacterium saccharophilum K-1 [Microbacterium saccharophilum]
3WPV_A	2.55e-197	76	583	8	488	Microbacteriumsaccharophilum K-1 beta-fructofuranosidase mutant T47S/F447V/F470Y/P500S [Microbacterium saccharophilum],3WPV_B Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/F447V/F470Y/P500S [Microbacterium saccharophilum],3WPV_C Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/F447V/F470Y/P500S [Microbacterium saccharophilum]
3WPY_A	2.55e-197	76	583	8	488	Microbacteriumsaccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447V/P500S [Microbacterium saccharophilum],3WPY_B Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447V/P500S [Microbacterium saccharophilum],3WPY_C Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447V/P500S [Microbacterium saccharophilum]
3WPZ_A	1.03e-196	76	583	8	488	Microbacteriumsaccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447P/F470Y/P500S [Microbacterium saccharophilum],3WPZ_B Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447P/F470Y/P500S [Microbacterium saccharophilum],3WPZ_C Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447P/F470Y/P500S [Microbacterium saccharophilum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q43998	2.44e-187	73	584	65	544	Levansucrase OS=Gluconacetobacter diazotrophicus OX=33996 GN=lsdA PE=1 SV=1
P0DJA3	2.99e-88	94	580	11	400	Levansucrase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacB PE=1 SV=1
F8DT26	2.99e-88	94	580	11	400	Levansucrase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1) OX=555217 GN=sacB PE=3 SV=1
P0DJA4	9.49e-87	94	582	7	400	Extracellular sucrase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacC PE=3 SV=1
F8DT27	9.49e-87	94	582	7	400	Extracellular sucrase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1) OX=555217 GN=sacC PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000766	0.998187	0.000331	0.000300	0.000219	0.000171

TMHMM  Annotations     

start	end
13	32