Species | Erysipelatoclostridium ramosum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium ramosum | |||||||||||
CAZyme ID | MGYG000001400_00587 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | Sucrose-6-phosphate hydrolase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 610042; End: 611442 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 26 | 333 | 9.7e-88 | 0.9965870307167235 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd18623 | GH32_ScrB-like | 7.70e-153 | 32 | 326 | 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. |
TIGR01322 | scrB_fam | 2.64e-138 | 9 | 439 | 1 | 443 | sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
COG1621 | SacC | 4.40e-137 | 7 | 452 | 14 | 471 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
smart00640 | Glyco_32 | 5.84e-104 | 26 | 430 | 1 | 437 | Glycosyl hydrolases family 32. |
pfam00251 | Glyco_hydro_32N | 3.35e-101 | 26 | 333 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QQV06328.1 | 0.0 | 1 | 466 | 1 | 466 |
QMW75218.1 | 0.0 | 1 | 466 | 1 | 466 |
QPS14445.1 | 0.0 | 1 | 466 | 1 | 466 |
QQY26690.1 | 0.0 | 1 | 466 | 1 | 466 |
CED94068.1 | 2.15e-158 | 9 | 465 | 15 | 480 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6NU7_A | 3.14e-64 | 12 | 456 | 23 | 479 | Structureof sucrose-6-phosphate hydrolase from Lactobacillus gasseri [Lactobacillus gasseri 224-1],6NU8_A Structure of sucrose-6-phosphate hydrolase from Lactobacillus gasseri in complex with fructose [Lactobacillus gasseri 224-1] |
7VCO_A | 1.30e-62 | 25 | 452 | 29 | 471 | ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara] |
7BWB_A | 1.30e-61 | 13 | 439 | 40 | 460 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori] |
7BWC_A | 1.90e-60 | 13 | 439 | 40 | 460 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori] |
1UYP_A | 5.57e-51 | 21 | 462 | 2 | 429 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P07819 | 7.14e-99 | 7 | 448 | 14 | 462 | Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2 |
Q05936 | 1.25e-79 | 7 | 465 | 19 | 489 | Sucrose-6-phosphate hydrolase OS=Staphylococcus xylosus OX=1288 GN=scrB PE=3 SV=1 |
P13394 | 1.88e-75 | 9 | 439 | 24 | 453 | Sucrose-6-phosphate hydrolase OS=Vibrio alginolyticus OX=663 GN=scrB PE=2 SV=1 |
A1STJ9 | 3.30e-74 | 20 | 454 | 94 | 529 | Probable sucrose-6-phosphate hydrolase OS=Psychromonas ingrahamii (strain 37) OX=357804 GN=Ping_0974 PE=3 SV=1 |
P40714 | 2.45e-69 | 9 | 449 | 13 | 459 | Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000063 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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