CAZyme Information: MGYG000003687_03789

Basic Information

• Species: Paenibacillus polymyxa
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
• CAZyme ID: MGYG000003687_03789
• CAZy Family: GH68
• CAZyme Description: Levansucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
170	MGYG000003687_17|CGC3	18869.3	6.2305

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003687	5656034	Isolate	China	Asia

• Gene Location: Start: 85404; End: 85916 Strand: -

Full Sequence      

MNDDYTLKNVMPPLLASNLVTDEIERANVFKMNGLWYLFTSTRGSKVTVDAIGDDDIYML
GYVSTSLTGPYKPLNGTGLVLHQDLDRDDITWTYAHFAIPQGKGNNVVVSSYMTNRGLFP
DHKSTFAPSFLLNIKGSKTSVVKNGILEQGQITIDPGNDKKDNQNEYGKK

Enzyme Prediction     

EC	2.4.1.10	3.2.1.26

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH68	2	152	5.5e-52	0.354916067146283

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam02435	Glyco_hydro_68	1.27e-63	2	144	271	411	Levansucrase/Invertase. This Pfam family consists of the glycosyl hydrolase 68 family, including several bacterial levansucrase enzymes, and invertase from zymomonas.
cd08997	GH68	5.56e-49	2	142	216	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.
cd08979	GH_J	4.74e-34	2	133	162	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.
cd18609	GH32-like	0.006	10	80	192	262	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPK52124.1	2.82e-118	1	170	330	499
AUS24949.1	2.82e-118	1	170	330	499
AIY10058.1	2.82e-118	1	170	330	499
AHM64394.1	2.82e-118	1	170	330	499
QDA26279.1	2.82e-118	1	170	330	499

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VDT_A	3.88e-82	1	154	285	438	Crystallographicstructure of Levansucrase from Bacillus subtilis mutant S164A [Bacillus subtilis]
1OYG_A	4.83e-82	1	154	292	445	Crystalstructure of Bacillus subtilis levansucrase [Bacillus subtilis]
6PWQ_A	8.04e-82	1	154	289	442	Crystalstructure of Levansucrase from Bacillus subtilis mutant S164A at 2.6 A [Bacillus subtilis],6PWQ_B Crystal structure of Levansucrase from Bacillus subtilis mutant S164A at 2.6 A [Bacillus subtilis]
3BYJ_A	9.67e-82	1	154	318	471	ChainA, Levansucrase [Bacillus subtilis]
3BYK_A	9.67e-82	1	154	318	471	ChainA, Levansucrase [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05655	5.30e-81	1	154	318	471	Levansucrase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacB PE=1 SV=1
P21130	1.16e-79	1	154	318	471	Levansucrase OS=Bacillus amyloliquefaciens OX=1390 GN=sacB PE=2 SV=1
P94468	8.39e-77	1	154	318	471	Inactive levansucrase OS=Geobacillus stearothermophilus OX=1422 GN=sacB PE=1 SV=1
Q55242	1.42e-30	13	150	535	682	Levansucrase OS=Streptococcus salivarius OX=1304 GN=ftf PE=3 SV=1
D3WYW0	5.05e-26	2	150	482	640	Levansucrase OS=Lactobacillus gasseri OX=1596 GN=levG PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000035	0.000006	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003687_03789.