CAZyme Information: MGYG000004763_02134

Basic Information

• Species: CAG-462 sp900291465
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-462; CAG-462 sp900291465
• CAZyme ID: MGYG000004763_02134
• CAZy Family: GH32
• CAZyme Description: Levanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
265	MGYG000004763_31|CGC1	30107.1	5.4644

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004763	3504022	MAG	Denmark	Europe

• Gene Location: Start: 37899; End: 38696 Strand: +

Full Sequence      

MSINPGGPFGGSATQYFVGDFDGKTFTCESRPEQVKWMDYGKDHYATVTWSGVPDGRHIA
MAWMSNWQYANEVPTKQFRSANALPRDLSLYRDEETGECFLSVLPVKEVESLRGRVQEYR
AFTASTRQVEKKLPQQWGDACEIVLELLPRSAEKTFIRLSNPDGEKVVMCYDRQSNTFSM
DRTQSGIMDFSRDFPAVTVAPCPGNGRLKLRLFLDRCSLEAFEADGRMVMTNLLFPNKPY
TMLSVYTESGSTRVWSLDIYEITGK

Enzyme Prediction     

EC	3.2.1.26	3.2.1.64	3.2.1.80	3.2.1.65	3.2.1.153

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1621	SacC	8.69e-51	1	254	239	477	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	4.60e-44	10	226	216	437	Glycosyl hydrolases family 32.
cd18622	GH32_Inu-like	9.58e-43	1	90	202	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.
pfam08244	Glyco_hydro_32C	1.09e-35	108	261	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.
pfam00251	Glyco_hydro_32N	1.36e-26	1	91	207	298	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM52398.1	5.67e-106	2	262	355	615
AVM58395.1	3.56e-104	2	262	355	615
BCS85428.1	2.89e-92	1	262	342	599
QCD40830.1	2.78e-89	2	263	338	599
QCP73719.1	2.78e-89	2	263	338	599

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	1.52e-36	3	262	245	513	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	2.02e-26	1	263	254	514	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]
6J0T_A	2.41e-26	1	263	270	552	Thecrystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042],6J0T_B The crystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042]
3KF3_A	2.59e-21	1	235	225	476	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	2.62e-21	1	235	228	479	ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05656	3.53e-53	1	262	245	509	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q96TU3	1.02e-35	3	262	264	532	Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
O31411	1.52e-35	11	262	622	875	Levanase (Fragment) OS=Bacillus sp. (strain L7) OX=62626 PE=1 SV=2
E1ABX2	3.71e-35	3	263	264	533	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
Q76HP6	3.71e-35	3	263	264	533	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE 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
1.000034	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004763_02134.