Species | Parabacteroides goldsteinii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides goldsteinii | |||||||||||
CAZyme ID | MGYG000001489_01903 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2547826; End: 2549823 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 408 | 640 | 1.4e-16 | 0.9475982532751092 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14791 | GH36 | 1.76e-13 | 282 | 548 | 5 | 278 | 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. |
pfam17801 | Melibiase_C | 6.10e-09 | 598 | 662 | 12 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
cd14792 | GH27 | 1.92e-06 | 282 | 573 | 4 | 268 | 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 |
---|---|---|---|---|---|
QJR69930.1 | 0.0 | 14 | 662 | 24 | 673 |
AII65845.1 | 0.0 | 14 | 662 | 24 | 673 |
QJR74262.1 | 0.0 | 14 | 662 | 24 | 673 |
QJR65668.1 | 0.0 | 14 | 662 | 24 | 673 |
AND18605.1 | 0.0 | 14 | 662 | 24 | 673 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q0CPK2 | 9.99e-06 | 444 | 661 | 160 | 401 | Probable alpha-galactosidase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglA PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000008 | 1.000060 | 0.000000 | 0.000000 | 0.000000 |
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