Species | UMGS1633 sp900553645 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UMGS1633; UMGS1633 sp900553645 | |||||||||||
CAZyme ID | MGYG000004044_02240 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 88; End: 2142 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH36 | 90 | 602 | 4e-91 | 0.7296511627906976 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14791 | GH36 | 2.07e-87 | 297 | 589 | 1 | 299 | glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. |
pfam02065 | Melibiase | 7.00e-39 | 262 | 597 | 2 | 347 | Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27. |
COG3345 | GalA | 8.04e-27 | 75 | 614 | 41 | 602 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
cd14792 | GH27 | 2.63e-05 | 302 | 380 | 5 | 84 | glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. |
cd06592 | GH31_NET37 | 6.58e-05 | 307 | 446 | 6 | 150 | glucosidase NET37. NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUC67017.1 | 0.0 | 1 | 682 | 1 | 683 |
QTE72326.1 | 0.0 | 1 | 682 | 1 | 683 |
QTE73314.1 | 0.0 | 1 | 682 | 1 | 683 |
QUA54327.1 | 0.0 | 5 | 683 | 8 | 687 |
QTE69360.1 | 1.31e-315 | 1 | 683 | 1 | 684 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4FNQ_A | 6.05e-31 | 256 | 678 | 284 | 714 | Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
4FNR_A | 1.42e-30 | 204 | 678 | 230 | 714 | Crystalstructure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_B Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_C Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_D Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
4FNP_A | 1.89e-30 | 204 | 678 | 230 | 714 | Crystalstructure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNS_A Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus] |
4FNT_A | 1.05e-29 | 204 | 678 | 230 | 714 | Crystalstructure of GH36 alpha-galactosidase AgaA A355E D548N from Geobacillus stearothermophilus in complex with raffinose [Geobacillus stearothermophilus],4FNT_B Crystal structure of GH36 alpha-galactosidase AgaA A355E D548N from Geobacillus stearothermophilus in complex with raffinose [Geobacillus stearothermophilus],4FNT_C Crystal structure of GH36 alpha-galactosidase AgaA A355E D548N from Geobacillus stearothermophilus in complex with raffinose [Geobacillus stearothermophilus],4FNT_D Crystal structure of GH36 alpha-galactosidase AgaA A355E D548N from Geobacillus stearothermophilus in complex with raffinose [Geobacillus stearothermophilus] |
4FNU_A | 2.45e-29 | 204 | 678 | 230 | 714 | Crystalstructure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus],4FNU_B Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus],4FNU_C Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus],4FNU_D Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9ALJ4 | 7.80e-30 | 204 | 678 | 230 | 714 | Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1 |
Q5ARP5 | 1.58e-25 | 116 | 519 | 161 | 553 | Probable alpha-galactosidase G OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aglG PE=2 SV=1 |
Q0CEF5 | 2.21e-21 | 170 | 503 | 184 | 536 | Probable alpha-galactosidase G OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglG PE=3 SV=1 |
Q0CVH2 | 2.29e-21 | 204 | 678 | 248 | 735 | Probable alpha-galactosidase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglC PE=3 SV=1 |
Q9UUZ4 | 7.01e-21 | 204 | 503 | 249 | 560 | Alpha-galactosidase C OS=Aspergillus niger OX=5061 GN=aglC PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000061 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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