CAZyme Information: MGYG000002326_03581

Basic Information

• Species: Alkalihalobacillus alcalophilus
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_H; Bacillaceae_D; Alkalihalobacillus; Alkalihalobacillus alcalophilus
• CAZyme ID: MGYG000002326_03581
• CAZy Family: GH32
• CAZyme Description: Levanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
300	MGYG000002326_247|CGC1	34323.12	3.9032

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002326	4217920	Isolate	not provided	not provided

• Gene Location: Start: 4960; End: 5862 Strand: -

Full Sequence      

MGSHLGVWECPDLFELAIDGDPDHTKWVLQVDIGDGAIAGGSGAQYFIGEFDGTTFVSDH
DPEQINWLDYGADFYAAQSFSDMPTEDGRRVMIAWMNNWLYANQVPTEVWRGAMSFPREM
QLMTDSMGEIKVAQKPIEELNSLRGEQLFYLENEKVDQSFAKELLADIKADTFELFIEID
RNSLSDVGFKIRQSDNLEDETQIGFSSETNELFVERRQLDEIYFSPYFNGRHKVEIANSN
TLTLQILVDQSSVEVFAQDGQYVITDLIFPNEDSVNMEFFLEGEEVFIHNLTIHSLQSIW

Enzyme Prediction     

No EC number prediction in MGYG000002326_03581.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	6	136	3.3e-36	0.3924914675767918

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1621	SacC	8.92e-67	1	274	211	463	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	6.21e-66	1	260	184	437	Glycosyl hydrolases family 32.
cd18622	GH32_Inu-like	4.45e-60	2	122	174	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.
pfam00251	Glyco_hydro_32N	3.09e-39	6	136	185	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.
pfam08244	Glyco_hydro_32C	2.11e-35	139	295	1	162	Glycosyl hydrolases family 32 C terminal. This domain corresponds to the C terminal domain of glycosyl hydrolase family 32. It forms a beta sandwich module.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAT54241.1	1.26e-86	2	300	216	513
AOP15995.1	1.26e-86	2	300	216	513
VEH79079.1	1.26e-86	2	300	216	513
QNH43727.1	1.26e-86	2	300	216	513
AVI46294.1	1.26e-86	2	300	216	513

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	2.31e-45	6	300	219	517	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]
3RWK_X	8.47e-41	1	296	225	513	Firstcrystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum],3SC7_X First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum]
4EQV_A	1.61e-28	8	277	202	493	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]
6J0T_A	1.02e-25	8	275	237	530	Thecrystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042],6J0T_B The crystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042]
3KF3_A	1.18e-23	2	272	197	479	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05656	5.57e-81	2	300	216	513	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
O31411	1.89e-55	6	300	588	879	Levanase (Fragment) OS=Bacillus sp. (strain L7) OX=62626 PE=1 SV=2
Q76HP6	4.37e-47	6	300	238	536	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1
E1ABX2	4.37e-47	6	300	238	536	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
A2R0E0	8.48e-47	6	300	238	536	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000067	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002326_03581.