CAZyme Information: MGYG000002123_02372

Basic Information

• Species: UMGS1696 sp900763885
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1696; UMGS1696 sp900763885
• CAZyme ID: MGYG000002123_02372
• CAZy Family: GH32
• CAZyme Description: Levanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
540		60293.42	4.694

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002123	2956735	MAG	Mongolia	Asia

• Gene Location: Start: 297; End: 1919 Strand: -

Full Sequence      

MLHTCCAANRYLVLPVVKAEANSKILFYQIAADGGRALVYDLDVAYAPEDPAATPMFVDL
GRFDGLTLAIERYPAIDRASADLDNPLPYTPVFAPERDRECCYHTAHRPMVHFTTRYGWI
NDPNGLTYADGVYHMFYQHNPAGLNWGNMHWGHAVSGDLIHWCEWGDALYPDAHGTMFSG
CGLPDPADHLGISDGQNTPLLFYYTAAAYQSMLSRGAVTAQYLAYSADGGRTLTKLPEPV
IPGETDGNRDPKIIWCEEMGCYVCALYMTGHEYHIYKTADLTRFTFVQKVILPDDAECPD
LYPLTCGGERFWIFSGASDTYLVGKMTRDGFHPVQDAQYYRLGGGGSYAAQTFSGIDDRR
IKVAWGQMEAPDACFTSQMNFPTEVRLDCVDGKYRLATLPIAEIAQLRTDTRTWEKTASV
SNPLIDYLNGGAYEITIRFGKACAAMTVELYGLRLRILPEENILELPGRVLPLSYNYSGR
EVRLIIDTMSMEVFSDEGRIYTAEPCLPELQNRQFTLAPVKPMQVCEVAVSISPLGDIWE

Enzyme Prediction     

No EC number prediction in MGYG000002123_02372.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	112	391	3.6e-60	0.9726962457337884

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18622	GH32_Inu-like	3.15e-83	118	387	2	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	5.68e-67	112	498	1	402	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	1.41e-63	112	394	1	304	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	8.52e-62	105	504	26	456	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd08996	GH32_FFase	5.12e-59	118	387	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUS97079.1	6.92e-95	9	539	7	528
ARN56628.1	1.09e-76	8	501	206	696
QEG37372.1	5.01e-76	9	540	45	571
AMV32176.1	1.15e-75	9	539	205	732
QJE94510.1	2.18e-75	9	494	192	676

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	3.84e-32	103	400	3	352	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	1.32e-28	107	508	28	487	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	6.06e-27	107	365	9	284	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	6.21e-27	107	365	12	287	ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
7VCO_A	1.27e-26	109	517	27	468	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05656	5.02e-50	90	539	17	513	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q03174	1.60e-32	100	508	436	886	Fructan beta-fructosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=fruA PE=2 SV=2
A2R0E0	1.38e-31	103	400	22	371	Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1
E1ABX2	1.38e-31	103	400	22	371	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
Q76HP6	1.38e-31	103	400	22	371	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
0.999816	0.000217	0.000011	0.000001	0.000000	0.000002

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002123_02372.