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CAZyme Information: MGYG000002407_01531
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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 | Cohnella sp900169535 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Cohnella; Cohnella sp900169535 | |||||||||||
| CAZyme ID | MGYG000002407_01531 | |||||||||||
| CAZy Family | GH32 | |||||||||||
| CAZyme Description | Sucrose-6-phosphate hydrolase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 255882; End: 257411 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH32 | 32 | 334 | 2.1e-111 | 0.9829351535836177 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG1621 | SacC | 0.0 | 1 | 493 | 3 | 486 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
| TIGR01322 | scrB_fam | 5.01e-176 | 15 | 466 | 1 | 444 | sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
| cd18623 | GH32_ScrB-like | 2.01e-149 | 38 | 331 | 1 | 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. |
| smart00640 | Glyco_32 | 2.52e-149 | 32 | 456 | 1 | 437 | Glycosyl hydrolases family 32. |
| cd08996 | GH32_FFase | 2.08e-146 | 38 | 329 | 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 help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AXI30686.1 | 5.00e-218 | 2 | 491 | 6 | 493 |
| QIZ06176.1 | 2.24e-217 | 6 | 491 | 6 | 489 |
| ARK30083.1 | 4.71e-216 | 10 | 491 | 10 | 489 |
| AWD63555.1 | 1.80e-213 | 2 | 491 | 6 | 493 |
| QFY74357.1 | 1.80e-213 | 2 | 491 | 6 | 493 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7VCO_A | 3.37e-135 | 6 | 491 | 5 | 485 | ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara] |
| 7BWB_A | 7.86e-110 | 27 | 484 | 48 | 468 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori] |
| 7BWC_A | 1.24e-108 | 27 | 484 | 48 | 468 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori] |
| 3PIG_A | 8.70e-100 | 1 | 500 | 11 | 518 | 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 | 1.85e-96 | 27 | 500 | 39 | 518 | 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 | 5.15e-128 | 29 | 492 | 26 | 477 | Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1 |
| F8DVG5 | 7.02e-126 | 25 | 493 | 26 | 501 | 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 | 7.02e-126 | 25 | 493 | 26 | 501 | Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1 |
| P16553 | 5.20e-122 | 16 | 491 | 10 | 475 | Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1 |
| P07819 | 3.95e-101 | 28 | 479 | 29 | 467 | Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2 |
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 |
|---|---|---|---|---|---|
| 1.000044 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |