CAZyme Information: MGYG000000720_00437

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis
• CAZyme ID: MGYG000000720_00437
• CAZy Family: GH32
• CAZyme Description: Levanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
343	MGYG000000720_5|CGC1	39060.02	5.8884

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000720	3759035	MAG	Kazakhstan	Asia

• Gene Location: Start: 73592; End: 74623 Strand: -

Full Sequence      

MSQYKFSRPEYHFTVHRGWLNDPNGLIRLGNDYHMFFQHNPSAPDWGNMHWGHAVSSDLL
HWKELPVALKPKSPEDLCFSGSAILDTENASGFGSTENPPLLVYFTSTGRGECLAYSLDG
GLTFREYENNPVIRHNGRDPRVIQYAPGHYVIAVYDEVNHIAFYRSSDLKNWTFCSRIHG
FYECPELFQLGGRWVLFAGNGVYSIGRFDGETFTPETFPRPLFEGDAYAGQTFANCDRRI
AIFWLRDRKGIFREQGFSQQMSIPVELTMKEERILVNPAVEVPGSYVLSSPDRPVMIRGV
ELPAAEEILVVEDAATVEAFINHGERCILRYATEPLDPSLHRK

Enzyme Prediction     

No EC number prediction in MGYG000000720_00437.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	12	275	6.4e-72	0.9863481228668942

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18622	GH32_Inu-like	1.94e-111	17	269	1	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.
cd08996	GH32_FFase	7.88e-80	18	269	1	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.
pfam00251	Glyco_hydro_32N	1.27e-77	12	273	1	301	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.
COG1621	SacC	1.16e-75	8	282	29	340	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	2.55e-75	12	282	1	315	Glycosyl hydrolases family 32.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM45778.1	1.94e-209	8	340	7	338
AGA28800.1	1.46e-98	8	270	294	567
AMV40679.1	4.43e-91	8	270	279	556
QMU29466.1	9.69e-91	8	286	139	444
QEH38715.1	6.84e-90	8	270	126	401

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	7.73e-44	8	235	8	285	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	1.04e-43	8	216	29	282	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]
3KF3_A	4.85e-43	5	240	7	279	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	5.07e-43	5	240	10	282	ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
1UYP_A	2.62e-42	8	281	3	297	Thethree-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_B The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_C The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_D The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_E The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_F The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05656	9.80e-49	8	270	35	337	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
O42878	1.86e-45	8	269	4	312	Putative invertase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC8E11.01c PE=3 SV=3
Q76HP6	4.07e-45	8	235	27	304	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1
E1ABX2	4.07e-45	8	235	27	304	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
A2R0E0	5.63e-44	8	235	27	304	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 MGYG000000720_00437.