dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Bacillus paralicheniformis

Lineage

Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus paralicheniformis

CAZyme ID

MGYG000000147_01663

CAZy Family

GH32

CAZyme Description

Levanbiose-producing levanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
495		56342.78	4.5722

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000147	4371304	Isolate	United Kingdom	Europe

Gene Location

Start: 741777; End: 743264 Strand: -

Enzyme Prediction help

EC	3.2.1.65	3.2.1.64

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH32	26	327	7.6e-79	0.9761092150170648

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1621	SacC	1.13e-153	8	492	15	486	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd18622	GH32_Inu-like	1.60e-136	33	321	3	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.
smart00640	Glyco_32	1.68e-105	26	454	1	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	2.39e-100	26	335	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.
cd08996	GH32_FFase	3.71e-55	33	321	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 help

Hit ID	Query Start	Query End	Hit Start	Hit End
VEB20833.1	1	495	21	515
BAL45528.1	1	495	21	515
QAW39253.1	1	495	21	515
QFY37158.1	1	495	21	515
BCE16498.1	1	495	21	515

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4FFF_A	5.98e-109	23	490	2	478	CrystalStructure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens],4FFF_B Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens],4FFF_C Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens],4FFF_D Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens]
4FFG_A	6.35e-109	23	490	2	478	CrystalStructure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens],4FFG_B Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens],4FFG_C Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens],4FFG_D Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens]
4FFH_A	3.56e-108	23	490	2	478	CrystalStructure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFH_B Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFH_C Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFH_D Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFI_A Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens],4FFI_B Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens],4FFI_C Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens],4FFI_D Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens]
1Y4W_A	5.89e-55	21	478	7	501	Crystalstructure 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]
4EQV_A	2.74e-53	22	485	8	500	Structureof Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_B Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_C Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_D Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_E Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_F Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_G Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_H Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O07003	5.04e-261	3	495	25	516	Levanbiose-producing levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=levB PE=1 SV=1
P94469	1.62e-220	36	430	1	394	Levanbiose-producing levanase (Fragment) OS=Geobacillus stearothermophilus OX=1422 GN=levB PE=1 SV=2
P05656	2.74e-78	20	493	33	512	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
O31411	2.78e-61	18	493	394	878	Levanase (Fragment) OS=Bacillus sp. (strain L7) OX=62626 PE=1 SV=2
Q76HP6	1.73e-54	21	479	26	521	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.990554	0.009365	0.000054	0.000025	0.000013	0.000027

TMHMM Annotations help

There is no transmembrane helices in MGYG000000147_01663.

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