Species | Ruminococcus_D sp900770285 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_D; Ruminococcus_D sp900770285 | |||||||||||
CAZyme ID | MGYG000003587_00501 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 7262; End: 9373 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH36 | 77 | 643 | 1.2e-95 | 0.811046511627907 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14791 | GH36 | 1.53e-88 | 311 | 603 | 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 | 1.03e-28 | 323 | 605 | 54 | 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 | 2.19e-21 | 323 | 530 | 305 | 508 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
cd14792 | GH27 | 1.67e-08 | 313 | 473 | 5 | 137 | 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. |
cd07568 | ML_beta-AS_like | 0.001 | 327 | 387 | 30 | 92 | mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases). This family includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This family belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CCO06137.1 | 0.0 | 1 | 703 | 1 | 703 |
ADL52223.1 | 0.0 | 1 | 701 | 1 | 700 |
ADU21534.1 | 0.0 | 1 | 702 | 1 | 699 |
BCK00066.1 | 0.0 | 1 | 702 | 1 | 701 |
QHQ59595.1 | 0.0 | 1 | 702 | 1 | 701 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2XN0_A | 4.68e-23 | 93 | 606 | 137 | 634 | 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 | 6.19e-23 | 93 | 606 | 137 | 634 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
2YFN_A | 1.29e-14 | 198 | 635 | 215 | 652 | 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] |
6JHP_A | 3.02e-11 | 107 | 530 | 178 | 584 | 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 |
---|---|---|---|---|---|---|
G1UB44 | 2.56e-22 | 93 | 606 | 137 | 634 | Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1 |
P43467 | 6.82e-20 | 93 | 605 | 135 | 631 | Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1 |
P27756 | 4.00e-17 | 264 | 609 | 277 | 626 | Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3 |
P16551 | 3.62e-16 | 244 | 548 | 230 | 526 | Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA PE=1 SV=1 |
G4T4R7 | 8.38e-14 | 198 | 635 | 215 | 652 | Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000056 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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