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CAZyme Information: MGYG000000326_01557
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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 | Rothia terrae | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Rothia; Rothia terrae | |||||||||||
| CAZyme ID | MGYG000000326_01557 | |||||||||||
| CAZy Family | GH68 | |||||||||||
| CAZyme Description | Levansucrase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 73; End: 1089 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH68 | 2 | 315 | 2e-105 | 0.7050359712230215 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd08997 | GH68 | 2.26e-107 | 2 | 311 | 61 | 354 | Glycosyl hydrolase family 68, includes levansucrase, beta-fructofuranosidase and inulosucrase. Glycosyl hydrolase family 68 (GH68) consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Levansucrase, also known as beta-D-fructofuranosyl transferase, catalyzes the transfer of the sucrose fructosyl moiety to a growing levan chain. Similarly, inulosucrase catalyzes long inulin-type of fructans, and beta-fructofuranosidases create fructooligosaccharides (FOS). However, in the absence of high fructan/sucrose ratio, some GH68 enzymes can also use fructan as donor substrate. GH68 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. 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. Biotechnological applications of these enzymes include use of inulin in inexpensive production of rich fructose syrups as well as use of FOS as health-promoting pre-biotics. |
| pfam02435 | Glyco_hydro_68 | 5.86e-102 | 1 | 311 | 114 | 409 | Levansucrase/Invertase. This Pfam family consists of the glycosyl hydrolase 68 family, including several bacterial levansucrase enzymes, and invertase from zymomonas. |
| cd18609 | GH32-like | 1.52e-14 | 9 | 244 | 72 | 265 | Glycosyl hydrolase family 32 family protein. The GH32 family contains glycosyl hydrolase family GH32 proteins that cleave 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. |
| cd08996 | GH32_FFase | 8.69e-04 | 13 | 226 | 64 | 214 | 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 |
|---|---|---|---|---|---|
| QNV37317.1 | 4.46e-249 | 1 | 338 | 176 | 513 |
| QCR54872.1 | 1.52e-193 | 1 | 338 | 175 | 514 |
| AXK47045.1 | 1.16e-190 | 1 | 338 | 185 | 524 |
| QOT21977.1 | 9.18e-153 | 1 | 333 | 189 | 528 |
| BCW22464.1 | 1.64e-152 | 1 | 333 | 164 | 503 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1W18_A | 1.73e-121 | 1 | 334 | 142 | 487 | CrystalStructure of levansucrase from Gluconacetobacter diazotrophicus [Gluconacetobacter diazotrophicus],1W18_B Crystal Structure of levansucrase from Gluconacetobacter diazotrophicus [Gluconacetobacter diazotrophicus] |
| 6M0D_A | 5.59e-119 | 1 | 328 | 175 | 520 | Beijerinckiaindica beta-fructosyltransferase [Beijerinckia indica subsp. indica ATCC 9039],6M0E_A Beijerinckia indica beta-fructosyltransferase complexed with fructose [Beijerinckia indica subsp. indica ATCC 9039] |
| 3WPZ_A | 4.46e-117 | 1 | 329 | 151 | 488 | Microbacteriumsaccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447P/F470Y/P500S [Microbacterium saccharophilum],3WPZ_B Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447P/F470Y/P500S [Microbacterium saccharophilum],3WPZ_C Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447P/F470Y/P500S [Microbacterium saccharophilum] |
| 3VSR_A | 1.28e-116 | 1 | 329 | 151 | 488 | Microbacteriumsaccharophilum K-1 beta-fructofuranosidase catalytic domain [Microbacterium saccharophilum],3VSS_A Microbacterium saccharophilum K-1 beta-fructofuranosidase catalytic domain complexed with fructose [Microbacterium saccharophilum] |
| 3WPY_A | 3.57e-116 | 1 | 329 | 151 | 488 | Microbacteriumsaccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447V/P500S [Microbacterium saccharophilum],3WPY_B Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447V/P500S [Microbacterium saccharophilum],3WPY_C Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447V/P500S [Microbacterium saccharophilum] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q43998 | 1.44e-119 | 1 | 334 | 203 | 548 | Levansucrase OS=Gluconacetobacter diazotrophicus OX=33996 GN=lsdA PE=1 SV=1 |
| O54435 | 3.42e-73 | 4 | 329 | 122 | 410 | Levansucrase OS=Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / CIP 78.65) OX=745277 GN=sacB PE=3 SV=1 |
| O52408 | 1.50e-71 | 4 | 329 | 122 | 410 | Levansucrase OS=Pseudomonas savastanoi pv. glycinea OX=318 GN=lsc PE=3 SV=1 |
| O68609 | 2.30e-71 | 4 | 332 | 138 | 429 | Levansucrase OS=Pseudomonas savastanoi pv. phaseolicola OX=319 GN=lsc PE=3 SV=1 |
| Q46654 | 1.31e-69 | 9 | 332 | 127 | 413 | Levansucrase OS=Erwinia amylovora OX=552 GN=lsc 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 |
|---|---|---|---|---|---|
| 1.000054 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |