Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UMGS2037; | |||||||||||
CAZyme ID | MGYG000003578_03047 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | Alpha-galactosidase Mel36A | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 122; End: 1228 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH36 | 1 | 349 | 8.1e-155 | 0.502906976744186 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam02065 | Melibiase | 7.69e-157 | 1 | 274 | 74 | 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. |
cd14791 | GH36 | 2.77e-125 | 1 | 266 | 35 | 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. |
COG3345 | GalA | 1.33e-122 | 3 | 349 | 327 | 665 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
pfam16874 | Glyco_hydro_36C | 3.08e-27 | 288 | 365 | 1 | 78 | Glycosyl hydrolase family 36 C-terminal domain. This domain is found at the C-terminus of many family 36 glycoside hydrolases. It has a beta-sandwich structure with a Greek key motif. |
cd14792 | GH27 | 3.69e-09 | 2 | 49 | 40 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL12368.1 | 1.16e-201 | 1 | 368 | 148 | 515 |
AEN97404.1 | 2.63e-200 | 1 | 365 | 363 | 727 |
EEV02558.1 | 3.65e-199 | 1 | 368 | 361 | 728 |
VCV21221.1 | 3.65e-199 | 1 | 368 | 361 | 728 |
CBL10423.1 | 3.89e-199 | 1 | 368 | 361 | 728 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2XN0_A | 6.85e-130 | 1 | 367 | 366 | 730 | 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 | 1.37e-129 | 1 | 367 | 366 | 730 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
2YFN_A | 5.54e-129 | 1 | 352 | 362 | 704 | 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] |
4FNQ_A | 3.88e-125 | 1 | 367 | 362 | 726 | Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
4FNR_A | 6.10e-124 | 1 | 367 | 362 | 726 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
G1UB44 | 3.75e-129 | 1 | 367 | 366 | 730 | Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1 |
G4T4R7 | 6.10e-126 | 1 | 352 | 362 | 704 | Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK PE=1 SV=1 |
Q9ALJ4 | 3.34e-123 | 1 | 367 | 362 | 726 | Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1 |
P43467 | 8.86e-111 | 1 | 367 | 364 | 729 | Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1 |
P27756 | 1.98e-109 | 1 | 368 | 356 | 720 | Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000040 | 0.000007 | 0.000002 | 0.000000 | 0.000000 | 0.000000 |
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