Species | Bulleidia sp900539965 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Bulleidia; Bulleidia sp900539965 | |||||||||||
CAZyme ID | MGYG000000773_01023 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | 5-dehydro-2-deoxygluconokinase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 40751; End: 43165 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 37 | 347 | 2.8e-88 | 0.9965870307167235 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd18623 | GH32_ScrB-like | 5.52e-150 | 43 | 340 | 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 | 6.47e-131 | 22 | 452 | 3 | 443 | sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
COG1621 | SacC | 6.95e-122 | 3 | 469 | 18 | 469 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
cd01167 | bac_FRK | 3.52e-112 | 487 | 786 | 3 | 294 | Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate. |
pfam00251 | Glyco_hydro_32N | 7.35e-98 | 37 | 347 | 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 |
---|---|---|---|---|---|
AQP38736.1 | 1.59e-204 | 1 | 478 | 1 | 481 |
CBL38537.1 | 3.63e-203 | 1 | 478 | 1 | 481 |
QCP34478.1 | 8.35e-199 | 1 | 482 | 1 | 487 |
QMW71993.1 | 2.17e-196 | 1 | 482 | 1 | 487 |
BCD35034.1 | 2.17e-196 | 1 | 482 | 1 | 487 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7VCO_A | 1.75e-63 | 36 | 452 | 29 | 458 | ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara] |
6NU7_A | 4.32e-62 | 27 | 474 | 27 | 486 | 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] |
5EY7_A | 2.72e-49 | 490 | 800 | 25 | 322 | Crystalstructure of Fructokinase from Vibrio cholerae O395 in apo form [Vibrio cholerae O395],5EY7_B Crystal structure of Fructokinase from Vibrio cholerae O395 in apo form [Vibrio cholerae O395],5EYN_A Crystal structure of Fructokinase from Vibrio cholerae O395 in fructose, ADP, Beryllium trifluoride and calcium ion bound form [Vibrio cholerae O395],5F0Z_A Crystal structure of Fructokinase from Vibrio cholerae O395 in fructose, ADP and calcium ion bound form [Vibrio cholerae O395],5F11_A Crystal structure of Fructokinase from Vibrio cholerae O395 in fructose bound form [Vibrio cholerae O395] |
5YGG_A | 3.42e-48 | 490 | 800 | 25 | 322 | Crystalstructure of Fructokinase Double-Mutant (T261C-H108C) from Vibrio cholerae O395 in fructose, ADP and potassium ion bound form [Vibrio cholerae O395] |
7BWB_A | 6.48e-48 | 36 | 452 | 52 | 460 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P07819 | 2.30e-87 | 14 | 452 | 10 | 453 | Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2 |
Q05936 | 6.19e-79 | 3 | 452 | 8 | 463 | Sucrose-6-phosphate hydrolase OS=Staphylococcus xylosus OX=1288 GN=scrB PE=3 SV=1 |
P27217 | 1.14e-76 | 27 | 462 | 21 | 449 | Sucrose-6-phosphate hydrolase OS=Klebsiella pneumoniae OX=573 GN=scrB PE=1 SV=3 |
P37075 | 2.20e-76 | 27 | 452 | 21 | 438 | Sucrose-6-phosphate hydrolase OS=Salmonella typhimurium OX=90371 GN=scrB PE=3 SV=1 |
P13394 | 2.56e-76 | 28 | 452 | 32 | 453 | Sucrose-6-phosphate hydrolase OS=Vibrio alginolyticus OX=663 GN=scrB PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000064 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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