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CAZyme Information: MGYG000000674_00474
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; UMGS1810; UMGS1810; ; | |||||||||||
| CAZyme ID | MGYG000000674_00474 | |||||||||||
| CAZy Family | GH32 | |||||||||||
| CAZyme Description | Sucrose-6-phosphate hydrolase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 4313; End: 5608 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH32 | 5 | 314 | 2.1e-90 | 0.9931740614334471 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd08996 | GH32_FFase | 5.94e-114 | 12 | 304 | 2 | 279 | 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. |
| COG1621 | SacC | 4.21e-111 | 2 | 431 | 30 | 471 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
| cd18623 | GH32_ScrB-like | 5.65e-104 | 12 | 308 | 2 | 289 | glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase). Glycosyl hydrolase family GH32 subgroup contains sucrose-6-phosphate hydrolase (sucrase, EC:3.2.1.26) among others. The enzyme 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. 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. |
| TIGR01322 | scrB_fam | 1.40e-102 | 2 | 415 | 15 | 443 | sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
| pfam00251 | Glyco_hydro_32N | 1.44e-97 | 5 | 310 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| APO28255.1 | 3.40e-214 | 1 | 429 | 1 | 430 |
| ASM70696.1 | 4.32e-192 | 1 | 421 | 1 | 423 |
| CBL23209.1 | 4.33e-191 | 1 | 421 | 1 | 421 |
| AMP52092.1 | 7.80e-171 | 1 | 423 | 1 | 415 |
| AWY99338.1 | 2.90e-153 | 4 | 423 | 5 | 431 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7VCO_A | 4.54e-65 | 5 | 422 | 30 | 465 | ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara] |
| 7BWB_A | 9.59e-63 | 5 | 415 | 53 | 460 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori] |
| 7BWC_A | 1.42e-61 | 5 | 415 | 53 | 460 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori] |
| 3PIG_A | 1.58e-49 | 3 | 415 | 42 | 485 | beta-fructofuranosidasefrom Bifidobacterium longum [Bifidobacterium longum],3PIG_B beta-fructofuranosidase from Bifidobacterium longum [Bifidobacterium longum],3PIJ_A beta-fructofuranosidase from Bifidobacterium longum - complex with fructose [Bifidobacterium longum],3PIJ_B beta-fructofuranosidase from Bifidobacterium longum - complex with fructose [Bifidobacterium longum] |
| 6NUM_A | 3.69e-49 | 3 | 415 | 42 | 485 | Thestructure of GH32 from Bifidobacteium adolescentis [Bifidobacterium adolescentis],6NUN_A Structure of GH32 hydrolase from Bifidobacterium adolescentis in complex with frutose [Bifidobacterium adolescentis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P40714 | 2.74e-68 | 4 | 420 | 28 | 454 | Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1 |
| P07819 | 4.02e-63 | 2 | 411 | 30 | 449 | Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2 |
| F8DVG5 | 6.41e-62 | 4 | 424 | 32 | 481 | 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 | 2.46e-61 | 4 | 424 | 32 | 481 | Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1 |
| A1STJ9 | 2.63e-60 | 5 | 415 | 100 | 514 | Probable sucrose-6-phosphate hydrolase OS=Psychromonas ingrahamii (strain 37) OX=357804 GN=Ping_0974 PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000069 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |