Species | UMGS621 sp900543915 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UMGS621; UMGS621 sp900543915 | |||||||||||
CAZyme ID | MGYG000004221_01183 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 69717; End: 71849 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH36 | 100 | 655 | 2.8e-92 | 0.7805232558139535 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14791 | GH36 | 6.59e-82 | 317 | 609 | 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 | 5.53e-45 | 280 | 617 | 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 | 2.95e-32 | 270 | 619 | 243 | 594 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
cd14792 | GH27 | 2.29e-06 | 352 | 482 | 40 | 139 | 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 |
---|---|---|---|---|---|
ANS77143.1 | 5.94e-173 | 23 | 685 | 12 | 664 |
BBI32765.1 | 5.10e-160 | 25 | 656 | 38 | 657 |
QYM79268.1 | 3.62e-157 | 35 | 656 | 48 | 671 |
QNU68202.1 | 2.48e-153 | 3 | 674 | 3 | 661 |
QTE69360.1 | 2.63e-152 | 18 | 655 | 17 | 635 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2XN0_A | 6.85e-30 | 261 | 617 | 278 | 639 | 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 | 1.61e-29 | 261 | 617 | 278 | 639 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
3MI6_A | 3.73e-28 | 247 | 618 | 262 | 637 | 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] |
4FNQ_A | 6.01e-27 | 261 | 687 | 274 | 694 | Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
4FNR_A | 1.76e-25 | 261 | 687 | 274 | 694 | 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-29 | 261 | 617 | 278 | 639 | Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1 |
Q0CVH2 | 3.77e-28 | 139 | 690 | 185 | 724 | Probable alpha-galactosidase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglC PE=3 SV=1 |
P43467 | 3.48e-27 | 262 | 617 | 274 | 637 | Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1 |
B8NWY6 | 1.98e-26 | 139 | 690 | 189 | 728 | Probable alpha-galactosidase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aglC PE=3 SV=2 |
Q2TW69 | 1.98e-26 | 139 | 690 | 189 | 728 | Probable alpha-galactosidase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglC PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999955 | 0.000098 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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