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CAZyme Information: MGYG000000359_01914
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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; Lachnospirales; Lachnospiraceae; UBA7182; | |||||||||||
| CAZyme ID | MGYG000000359_01914 | |||||||||||
| CAZy Family | GH32 | |||||||||||
| CAZyme Description | Sucrose-6-phosphate hydrolase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1906; End: 3315 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH32 | 30 | 339 | 7.2e-88 | 0.9965870307167235 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd18623 | GH32_ScrB-like | 1.77e-155 | 36 | 332 | 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 | 2.27e-130 | 25 | 447 | 13 | 444 | sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
| COG1621 | SacC | 2.28e-122 | 1 | 469 | 1 | 481 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
| pfam00251 | Glyco_hydro_32N | 5.92e-105 | 30 | 339 | 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. |
| cd08996 | GH32_FFase | 2.60e-92 | 36 | 330 | 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 |
|---|---|---|---|---|---|
| QUO23081.1 | 1.05e-296 | 1 | 469 | 1 | 468 |
| ADZ81804.1 | 6.41e-161 | 1 | 457 | 1 | 463 |
| QEH67471.1 | 5.96e-159 | 1 | 457 | 1 | 463 |
| CBL24955.1 | 3.68e-158 | 1 | 458 | 1 | 465 |
| CCG34775.1 | 3.94e-158 | 1 | 462 | 1 | 471 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7VCO_A | 5.85e-72 | 24 | 459 | 24 | 471 | ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara] |
| 7BWB_A | 7.18e-62 | 14 | 462 | 34 | 476 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori] |
| 7BWC_A | 1.05e-60 | 14 | 462 | 34 | 476 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori] |
| 6NUM_A | 1.21e-54 | 20 | 462 | 34 | 501 | Thestructure of GH32 from Bifidobacteium adolescentis [Bifidobacterium adolescentis],6NUN_A Structure of GH32 hydrolase from Bifidobacterium adolescentis in complex with frutose [Bifidobacterium adolescentis] |
| 6NU7_A | 3.61e-53 | 36 | 446 | 43 | 462 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P07819 | 7.43e-93 | 6 | 460 | 11 | 467 | Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2 |
| P27217 | 2.05e-85 | 27 | 447 | 28 | 439 | Sucrose-6-phosphate hydrolase OS=Klebsiella pneumoniae OX=573 GN=scrB PE=1 SV=3 |
| P16553 | 5.89e-84 | 1 | 450 | 5 | 452 | Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1 |
| P13394 | 8.03e-83 | 5 | 465 | 13 | 480 | Sucrose-6-phosphate hydrolase OS=Vibrio alginolyticus OX=663 GN=scrB PE=2 SV=1 |
| P40714 | 1.22e-79 | 1 | 451 | 6 | 454 | Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA 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 |
|---|---|---|---|---|---|
| 1.000045 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |