Species | Firm-07 sp900548735 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; Firm-07; Firm-07 sp900548735 | |||||||||||
CAZyme ID | MGYG000000520_00803 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 7310; End: 9493 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH36 | 80 | 709 | 3.1e-73 | 0.8837209302325582 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14791 | GH36 | 2.22e-58 | 335 | 617 | 17 | 298 | 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 | 3.66e-42 | 339 | 619 | 60 | 340 | 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 | 9.50e-30 | 93 | 622 | 84 | 587 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
cd14792 | GH27 | 4.98e-09 | 336 | 405 | 21 | 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. |
pfam16499 | Melibiase_2 | 6.69e-07 | 328 | 406 | 26 | 96 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AZN41467.1 | 2.30e-124 | 24 | 727 | 17 | 711 |
AEE97820.1 | 1.57e-122 | 23 | 725 | 6 | 689 |
QNI33977.1 | 5.15e-47 | 53 | 726 | 15 | 672 |
VEG22793.1 | 8.61e-38 | 183 | 697 | 180 | 684 |
ADB08818.1 | 8.61e-38 | 183 | 697 | 180 | 684 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2XN2_A | 1.34e-24 | 339 | 558 | 352 | 571 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
2XN0_A | 1.34e-24 | 339 | 558 | 352 | 571 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN0_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN1_A Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_C Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_D Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM] |
3MI6_A | 6.42e-22 | 337 | 701 | 347 | 712 | ChainA, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_B Chain B, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_C Chain C, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_D Chain D, Alpha-galactosidase [Levilactobacillus brevis ATCC 367] |
4FNR_A | 1.44e-21 | 189 | 587 | 199 | 599 | 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] |
2YFN_A | 7.54e-21 | 199 | 708 | 209 | 701 | galactosidasedomain of alpha-galactosidase-sucrose kinase, AgaSK [[Ruminococcus] gnavus E1],2YFO_A GALACTOSIDASE DOMAIN OF ALPHA-GALACTOSIDASE-SUCROSE KINASE, AGASK, in complex with galactose [[Ruminococcus] gnavus E1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P43469 | 3.61e-27 | 339 | 606 | 342 | 611 | Alpha-galactosidase 2 OS=Pediococcus pentosaceus OX=1255 GN=agaS PE=3 SV=1 |
P16551 | 3.00e-24 | 339 | 560 | 311 | 526 | Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA PE=1 SV=1 |
G1UB44 | 7.36e-24 | 339 | 558 | 352 | 571 | Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1 |
Q0CEF5 | 1.57e-22 | 123 | 575 | 145 | 582 | Probable alpha-galactosidase G OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglG PE=3 SV=1 |
Q5AU92 | 5.04e-22 | 188 | 723 | 220 | 747 | Alpha-galactosidase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aglC PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000060 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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