Species | Actinomyces urogenitalis | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinomyces; Actinomyces urogenitalis | |||||||||||
CAZyme ID | MGYG000002900_00374 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 54739; End: 55566 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 7 | 241 | 5.2e-34 | 0.7372013651877133 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd18609 | GH32-like | 3.14e-105 | 3 | 261 | 34 | 300 | 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. |
cd08995 | GH32_EcAec43-like | 2.43e-36 | 15 | 217 | 34 | 221 | Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2). This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 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). GH32 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. |
cd08996 | GH32_FFase | 4.69e-25 | 14 | 240 | 35 | 248 | 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. |
350093 | cd08979 | 1.04e-24 | 3 | 215 | 21 | 224 | GH_J Glycosyl hydrolase families 32 and 68, which form the clan GH-J. This glycosyl hydrolase family clan J (according to carbohydrate-active enzymes database (CAZY)) includes family 32 (GH32) and 68 (GH68). GH32 enzymes include invertase (EC 3.2.1.26) and other 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.-). The GH68 family consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10, also known as beta-D-fructofuranosyl transferase), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9). GH32 and GH68 family enzymes are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) and 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. |
COG1621 | SacC | 1.96e-19 | 14 | 274 | 73 | 337 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AMD87790.1 | 3.74e-142 | 1 | 272 | 33 | 304 |
VEG26658.1 | 1.88e-137 | 1 | 271 | 33 | 302 |
CED91167.1 | 1.81e-133 | 1 | 272 | 33 | 303 |
QHO91084.1 | 1.52e-129 | 1 | 273 | 33 | 304 |
BDA63185.1 | 1.41e-125 | 1 | 273 | 33 | 304 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7BJ4_A | 2.91e-07 | 4 | 250 | 78 | 362 | ChainA, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_B Chain B, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_C Chain C, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_D Chain D, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_E Chain E, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_F Chain F, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_G Chain G, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_H Chain H, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_I Chain I, Levansucrase [Halalkalicoccus jeotgali B3],7BJ4_J Chain J, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_A Chain A, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_B Chain B, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_C Chain C, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_D Chain D, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_E Chain E, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_F Chain F, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_G Chain G, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_H Chain H, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_I Chain I, Levansucrase [Halalkalicoccus jeotgali B3],7BJ5_J Chain J, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_A Chain A, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_B Chain B, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_C Chain C, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_D Chain D, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_E Chain E, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_F Chain F, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_G Chain G, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_H Chain H, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_I Chain I, Levansucrase [Halalkalicoccus jeotgali B3],7BJC_J Chain J, Levansucrase [Halalkalicoccus jeotgali B3] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P29001 | 1.91e-06 | 14 | 162 | 160 | 297 | Acid beta-fructofuranosidase OS=Vigna radiata var. radiata OX=3916 GN=INVA PE=1 SV=1 |
Q43857 | 3.39e-06 | 14 | 154 | 152 | 279 | Acid beta-fructofuranosidase OS=Vicia faba OX=3906 GN=VCINV PE=2 SV=1 |
O24509 | 3.41e-06 | 14 | 158 | 160 | 293 | Acid beta-fructofuranosidase OS=Phaseolus vulgaris OX=3885 PE=2 SV=1 |
Q8W4S6 | 4.29e-06 | 4 | 156 | 53 | 197 | Beta-fructofuranosidase, insoluble isoenzyme CWINV6 OS=Arabidopsis thaliana OX=3702 GN=CWINV6 PE=2 SV=1 |
P93761 | 4.53e-06 | 10 | 63 | 152 | 203 | Acid beta-fructofuranosidase AIV-18 OS=Capsicum annuum OX=4072 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000032 | 0.000040 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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