Species | UBA7741 sp900314575 | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Atopobiaceae; UBA7741; UBA7741 sp900314575 | |||||||||||
CAZyme ID | MGYG000004755_01535 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | Alpha-galactosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 258; End: 2384 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH36 | 6 | 647 | 2.9e-182 | 0.9723837209302325 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam02065 | Melibiase | 1.85e-131 | 247 | 582 | 1 | 341 | 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 | 1.09e-114 | 66 | 665 | 69 | 677 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
cd14791 | GH36 | 5.47e-111 | 282 | 580 | 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. |
pfam16875 | Glyco_hydro_36N | 3.68e-22 | 24 | 243 | 3 | 256 | Glycosyl hydrolase family 36 N-terminal domain. This domain is found at the N-terminus of many family 36 glycoside hydrolases. It has a beta-supersandwich fold. |
cd14792 | GH27 | 5.08e-13 | 288 | 364 | 6 | 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 |
---|---|---|---|---|---|
QDB79036.1 | 8.45e-211 | 2 | 690 | 38 | 739 |
ACQ81061.1 | 4.70e-204 | 3 | 690 | 15 | 715 |
QQT13625.1 | 1.32e-198 | 7 | 690 | 10 | 706 |
ACZ23052.1 | 1.73e-198 | 7 | 702 | 4 | 704 |
QQU07933.1 | 1.87e-198 | 7 | 690 | 10 | 706 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2XN0_A | 2.91e-80 | 202 | 643 | 248 | 694 | 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 | 7.80e-80 | 202 | 643 | 248 | 694 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
3MI6_A | 7.21e-79 | 95 | 654 | 123 | 705 | 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 | 1.40e-76 | 112 | 654 | 152 | 701 | 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] |
4FNQ_A | 3.74e-76 | 112 | 654 | 152 | 701 | Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P16551 | 2.03e-131 | 25 | 699 | 24 | 705 | Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA PE=1 SV=1 |
G1UB44 | 1.59e-79 | 202 | 643 | 248 | 694 | Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1 |
Q9ALJ4 | 7.66e-76 | 112 | 654 | 152 | 701 | Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1 |
Q0CVH2 | 5.40e-74 | 125 | 685 | 183 | 731 | Probable alpha-galactosidase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglC PE=3 SV=1 |
Q5ARP5 | 1.33e-72 | 123 | 644 | 162 | 692 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000043 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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