CAZyme Information: MGYG000000227_01497

Basic Information

• Species: Bacillus sonorensis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus sonorensis
• CAZyme ID: MGYG000000227_01497
• CAZy Family: GH32
• CAZyme Description: Levanbiose-producing levanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
510		57777.19	6.1525

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000227	4782975	Isolate	China	Asia

• Gene Location: Start: 490967; End: 492499 Strand: -

Full Sequence      

MNQKMFVLSICAGIFMAMLLPASQTEKTEKTQKTQSGSTYRAAFHLTTPDKWKNDPQKPV
YFNGKYHYYYLYNRDYPKGNGTEWRHASSSDLVHWEDEGVAIPKYTNKNGDPWSGSVVVD
SNNTAGFGKGAIVAIMTQPSADSGKEEQFLWYSTNGGKTFAPYGEKPVLANPGSVDFRDP
KVIWDEQEQKWVMALAEGTKIGFYESRNLKEWRYTGGFQTNNIGIVECPDLFKMRANDGT
YKWVLGASANAKPSGKPNTFAYWTGSYNGKDFAADHEEPQWLDYGFDWYAGVTFEDGESS
DKYAKRYALAWMNNWDYSNDTPTEQEGFNGTDSIVRQLQLKHYEDNIYSLASQPISQLDK
LTVSTEYDEKIKVNGSKTLPVKGDTYRLDADISWSDIKNVGIRLRESENQKRHIDAGIFV
QGGYSYVNRGFTGQPDSTRTYLESRAPFDASKKKAHITVIVDKTTVELFIDDGRITQSNQ
AFPKLHDKGITLFTENGTAVFEHLTVKHFE

Enzyme Prediction     

EC	3.2.1.65	3.2.1.64

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	45	347	4.9e-76	0.9829351535836177

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1621	SacC	1.06e-155	22	510	12	485	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd18622	GH32_Inu-like	2.35e-132	52	340	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	1.39e-103	45	473	1	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	1.22e-97	45	349	1	306	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	3.95e-54	52	340	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
ASB87253.1	0.0	1	510	1	510
ATH93281.1	1.73e-314	3	510	7	511
SCA87925.1	8.86e-312	3	510	5	509
QAT67083.1	9.55e-312	3	510	7	511
QHZ45499.1	1.30e-303	3	509	7	510

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4FFF_A	1.22e-109	42	507	2	476	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	1.29e-109	42	507	2	476	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	7.24e-109	42	507	2	476	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]
4EQV_A	7.34e-54	41	482	8	481	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]
1Y4W_A	8.25e-54	40	498	7	502	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O07003	5.19e-260	40	510	43	512	Levanbiose-producing levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=levB PE=1 SV=1
P94469	7.70e-218	55	449	1	394	Levanbiose-producing levanase (Fragment) OS=Geobacillus stearothermophilus OX=1422 GN=levB PE=1 SV=2
P05656	5.35e-80	40	506	34	506	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
O31411	4.61e-59	40	497	397	863	Levanase (Fragment) OS=Bacillus sp. (strain L7) OX=62626 PE=1 SV=2
A2R0E0	3.37e-54	40	483	26	506	Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 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
0.011014	0.534201	0.453962	0.000308	0.000252	0.000237

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000227_01497.