Species | CAG-791 sp000431495 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-791; CAG-791 sp000431495 | |||||||||||
CAZyme ID | MGYG000000600_00546 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | Levanase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 67633; End: 68985 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 13 | 307 | 5.1e-60 | 0.9761092150170648 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd18622 | GH32_Inu-like | 7.07e-98 | 19 | 301 | 2 | 289 | glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes 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). 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. |
COG1621 | SacC | 2.46e-63 | 1 | 421 | 21 | 449 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
pfam00251 | Glyco_hydro_32N | 4.12e-59 | 13 | 312 | 1 | 306 | 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. |
smart00640 | Glyco_32 | 6.41e-59 | 13 | 312 | 1 | 309 | Glycosyl hydrolases family 32. |
cd08996 | GH32_FFase | 5.12e-54 | 19 | 301 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCN32675.1 | 8.78e-114 | 9 | 430 | 95 | 500 |
CBL10226.1 | 2.51e-106 | 2 | 431 | 110 | 538 |
VCV24083.1 | 9.96e-106 | 9 | 431 | 117 | 538 |
CBL13463.1 | 1.40e-105 | 9 | 431 | 117 | 538 |
ANU53177.1 | 1.14e-94 | 8 | 431 | 87 | 466 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3KF3_A | 2.93e-36 | 9 | 279 | 10 | 284 | ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis] |
3KF5_A | 3.04e-36 | 9 | 279 | 13 | 287 | ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis] |
3U75_A | 2.63e-35 | 9 | 279 | 36 | 310 | ChainA, Fructofuranosidase [Schwanniomyces occidentalis],3U75_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],3U75_C Chain C, Fructofuranosidase [Schwanniomyces occidentalis],3U75_D Chain D, Fructofuranosidase [Schwanniomyces occidentalis] |
3U14_A | 4.92e-35 | 9 | 279 | 36 | 310 | ChainA, Fructofuranosidase [Schwanniomyces occidentalis],3U14_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis] |
1Y4W_A | 1.76e-33 | 8 | 301 | 7 | 339 | Crystalstructure of exo-inulinase from Aspergillus awamori in spacegroup P21 [Aspergillus awamori],1Y9G_A Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose [Aspergillus awamori],1Y9M_A Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 [Aspergillus awamori] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P05656 | 1.71e-41 | 8 | 246 | 34 | 273 | Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1 |
O42878 | 1.04e-38 | 9 | 312 | 4 | 328 | Putative invertase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC8E11.01c PE=3 SV=3 |
P40912 | 1.10e-36 | 9 | 279 | 28 | 309 | Invertase OS=Wickerhamomyces anomalus OX=4927 GN=INV1 PE=3 SV=1 |
A5DHM6 | 1.85e-36 | 9 | 279 | 20 | 296 | Extracellular exo-inulinase OS=Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) OX=294746 GN=PGUG_02777 PE=1 SV=2 |
Q6BJW6 | 4.45e-36 | 9 | 279 | 35 | 309 | Invertase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=INV PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000057 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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