Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; | |||||||||||
CAZyme ID | MGYG000004197_01517 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 22760; End: 24820 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH36 | 79 | 650 | 6.7e-76 | 0.8226744186046512 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14791 | GH36 | 1.96e-50 | 297 | 503 | 10 | 211 | 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 | 1.32e-29 | 304 | 515 | 56 | 273 | 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 | 3.11e-26 | 180 | 647 | 185 | 649 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
COG1501 | YicI | 1.55e-07 | 304 | 483 | 278 | 455 | Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism]. |
cd14792 | GH27 | 3.68e-07 | 298 | 377 | 9 | 82 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGA24197.1 | 0.0 | 21 | 686 | 27 | 692 |
QGA23301.1 | 6.16e-287 | 32 | 681 | 42 | 688 |
QGA24711.1 | 1.04e-280 | 34 | 685 | 7 | 662 |
QDH53808.1 | 4.47e-279 | 24 | 681 | 28 | 689 |
QNL40259.1 | 7.31e-278 | 24 | 681 | 28 | 689 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6JHP_A | 3.28e-27 | 90 | 676 | 169 | 750 | Crystalstructure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],6JHP_B Crystal structure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],6JHP_C Crystal structure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],6JHP_D Crystal structure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'] |
3MI6_A | 1.30e-26 | 75 | 520 | 127 | 567 | 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] |
2XN0_A | 1.08e-23 | 168 | 511 | 213 | 552 | 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] |
2XN2_A | 2.50e-23 | 168 | 511 | 213 | 552 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
2YFN_A | 3.04e-22 | 207 | 644 | 253 | 682 | 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 |
---|---|---|---|---|---|---|
Q5AU92 | 3.24e-27 | 90 | 649 | 161 | 719 | 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 |
P43467 | 1.69e-26 | 311 | 644 | 353 | 692 | Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1 |
Q9UUZ4 | 6.82e-25 | 90 | 649 | 158 | 716 | Alpha-galactosidase C OS=Aspergillus niger OX=5061 GN=aglC PE=1 SV=1 |
P16551 | 8.27e-25 | 159 | 511 | 166 | 505 | Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA PE=1 SV=1 |
Q0CEF5 | 1.08e-23 | 90 | 646 | 135 | 691 | Probable alpha-galactosidase G OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglG PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000573 | 0.571402 | 0.427269 | 0.000270 | 0.000250 | 0.000212 |
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