| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; ; | |||||||||||
| CAZyme ID | MGYG000004727_01448 | |||||||||||
| CAZy Family | GH36 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 52; End: 2172 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH36 | 74 | 652 | 1.3e-92 | 0.8284883720930233 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14791 | GH36 | 1.16e-83 | 312 | 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 | 9.31e-27 | 287 | 605 | 13 | 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 | 8.98e-22 | 324 | 530 | 305 | 508 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
| pfam16875 | Glyco_hydro_36N | 5.29e-06 | 95 | 176 | 105 | 178 | 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 | 1.07e-04 | 338 | 387 | 33 | 80 | 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 |
|---|---|---|---|---|---|
| ADL52223.1 | 0.0 | 5 | 706 | 4 | 703 |
| QBE95776.1 | 0.0 | 5 | 703 | 4 | 700 |
| QIB55801.1 | 0.0 | 5 | 703 | 4 | 700 |
| QMW76333.1 | 0.0 | 5 | 703 | 4 | 700 |
| BCK00066.1 | 0.0 | 5 | 702 | 4 | 699 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2XN0_A | 3.58e-23 | 98 | 605 | 141 | 633 | 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 | 3.58e-23 | 98 | 605 | 141 | 633 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
| 6PHU_A | 2.39e-21 | 312 | 558 | 345 | 603 | SpAgawild type apo structure [Streptococcus pneumoniae TIGR4],6PHV_A Chain A, Alpha-galactosidase [Streptococcus pneumoniae TIGR4] |
| 6PHW_A | 9.63e-21 | 312 | 558 | 345 | 603 | ChainA, Alpha-galactosidase [Streptococcus pneumoniae TIGR4],6PHX_A SpAga D472N structure in complex with raffinose [Streptococcus pneumoniae TIGR4],6PHY_A Chain A, Alpha-galactosidase [Streptococcus pneumoniae TIGR4],6PI0_A AgaD472N-Linear Blood group B type 2 trisaccharide complex structure [Streptococcus pneumoniae TIGR4] |
| 2YFN_A | 5.14e-17 | 199 | 653 | 215 | 660 | 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] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| G1UB44 | 1.96e-22 | 98 | 605 | 141 | 633 | Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1 |
| P27756 | 1.79e-21 | 76 | 605 | 112 | 622 | Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3 |
| Q0CVH2 | 3.45e-18 | 96 | 547 | 153 | 589 | Probable alpha-galactosidase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglC PE=3 SV=1 |
| Q5AU92 | 2.41e-17 | 96 | 552 | 157 | 603 | Alpha-galactosidase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aglC PE=1 SV=1 |
| G4T4R7 | 3.43e-16 | 199 | 653 | 215 | 660 | 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 |
|---|---|---|---|---|---|
| 1.000032 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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