Species | Paenibacillus_A rubinfantis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A rubinfantis | |||||||||||
CAZyme ID | MGYG000001525_01422 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 436881; End: 438980 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH36 | 5 | 653 | 2.6e-97 | 0.9563953488372093 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14791 | GH36 | 3.55e-91 | 305 | 596 | 4 | 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 | 2.91e-30 | 289 | 510 | 27 | 250 | 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 | 8.27e-20 | 288 | 520 | 277 | 505 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
cd14792 | GH27 | 1.56e-09 | 331 | 470 | 33 | 140 | 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 | 5.50e-05 | 332 | 387 | 45 | 98 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QMV41922.1 | 0.0 | 3 | 695 | 4 | 694 |
QJD85481.1 | 0.0 | 6 | 697 | 7 | 698 |
QQZ59050.1 | 0.0 | 3 | 696 | 5 | 696 |
CQR54700.1 | 0.0 | 3 | 696 | 5 | 696 |
AFH62765.1 | 0.0 | 2 | 699 | 3 | 702 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2XN0_A | 2.63e-23 | 91 | 506 | 137 | 538 | 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 | 3.49e-23 | 91 | 506 | 137 | 538 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
4FNQ_A | 7.50e-22 | 240 | 675 | 267 | 701 | Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
3MI6_A | 1.16e-19 | 244 | 506 | 272 | 535 | 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] |
6JHP_A | 1.60e-16 | 195 | 540 | 249 | 601 | 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'] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P43467 | 2.03e-23 | 61 | 509 | 106 | 539 | Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1 |
G1UB44 | 1.44e-22 | 91 | 506 | 137 | 538 | Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1 |
P27756 | 2.65e-19 | 195 | 510 | 213 | 531 | Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3 |
Q0CVH2 | 1.24e-16 | 196 | 545 | 237 | 599 | Probable alpha-galactosidase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglC PE=3 SV=1 |
P43469 | 4.79e-16 | 236 | 656 | 262 | 679 | Alpha-galactosidase 2 OS=Pediococcus pentosaceus OX=1255 GN=agaS PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000072 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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