CAZyme Information: MGYG000000123_03694

Basic Information

• Species: Blautia sp001304935
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp001304935
• CAZyme ID: MGYG000000123_03694
• CAZy Family: GH32
• CAZyme Description: Beta-fructosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
554	MGYG000000123_12|CGC3	63925.78	4.629

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000123	5803260	Isolate	Canada	North America

• Gene Location: Start: 86566; End: 88230 Strand: -

Full Sequence      

MIQTGEYTCLEIMTRTVEGKKGYVVLRDKEGRENRYEAGKKYYQWLKIPVERQSSYELTS
RDAEISLAYLSGCENILEKGICFIEPADGGISLSSREAAAYYDTPYREQYHFAPWKNWMN
DPNGLCWYQGYYHMYYQYNPHGQEWSNMYWGHAASPDLVHWTHLPVVLEPQKEVLEQADI
RKGGAFSGSAVVLDDETVFYLTRHLGPMEDGEETVQQQWMTRSRDMLEFEPEKLVIGEHP
VGASFDFRDPKVLKVGDVWYMVLASAVDGQAAILLYRSEDMEHWDYVKPLVTEPEEGVRC
FECPDFFPLDGSFTAWGALMCHRDVYGRYQMSRYYIGEFRDENFTVKSTGWFDFGSNCYA
MQSFEHEGRRIAIGWISDFYGEHVEVENGAYGSMTIPRVLHVKNDRLYMTPAEEIYTLKS
ERLYTGEKENIHLEHIAGNSFYSEITFSENTDFNLLLGRDGKKEIRFIKEKDFAGICTSG
VKSEGISFPADVDMVRDMEIFVDRRAVEIFINGGEAAGTKLFYNSGTEGCFVLEAERPEA
VTRAEVTKMQSVWQ

Enzyme Prediction     

No EC number prediction in MGYG000000123_03694.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	111	411	8.2e-83	0.9965870307167235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18625	GH32_BfrA-like	1.32e-156	117	402	1	286	glycoside hydrolase family 32 protein such as Thermotoga maritima invertase (BfrA or Tm1414). This subfamily of glycosyl hydrolase family GH32 includes beta-fructosidase (invertase, EC 3.2.1.26) that 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. 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. 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.
COG1621	SacC	4.37e-93	101	523	23	458	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd08996	GH32_FFase	6.71e-90	117	402	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.
smart00640	Glyco_32	1.09e-89	111	514	1	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	1.21e-84	111	411	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJU15047.1	0.0	1	554	1	554
QQQ92399.1	0.0	1	554	1	554
ASU27660.1	0.0	1	554	1	554
ANU74851.1	0.0	1	554	1	554
QBE99253.1	0.0	1	554	1	554

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6NOB_A	8.88e-83	48	553	57	636	Structureof Glycoside Hydrolase family 32 from Bifidobacterium adolescentis [Bifidobacterium adolescentis ATCC 15703]
1UYP_A	2.30e-56	106	553	2	431	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]
7VCO_A	3.14e-56	106	536	25	471	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
1W2T_A	6.22e-56	106	553	2	431	beta-fructosidasefrom Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_B beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_C beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_D beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_E beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_F beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8]
7BWB_A	4.20e-54	106	429	48	367	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33833	1.26e-55	106	553	2	431	Beta-fructosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bfrA PE=1 SV=1
F8DVG5	9.66e-51	110	518	32	463	Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1) OX=555217 GN=sacA PE=3 SV=1
P0DJA7	9.43e-50	110	518	32	463	Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1
P40714	1.63e-46	110	541	28	467	Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1
P05656	5.56e-45	99	553	27	513	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC 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
1.000085	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000123_03694.