You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000004193_01380
You are here: Home > Sequence: MGYG000004193_01380
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; UMGS1810; UMGS1810; NSJ-50; | |||||||||||
| CAZyme ID | MGYG000004193_01380 | |||||||||||
| CAZy Family | GH36 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 1755; End: 3725 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH36 | 138 | 639 | 6.7e-66 | 0.7267441860465116 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14791 | GH36 | 4.00e-39 | 258 | 467 | 11 | 211 | 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 | 4.08e-27 | 287 | 475 | 77 | 260 | 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 | 9.32e-27 | 153 | 653 | 185 | 680 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
| cd06589 | GH31 | 1.37e-05 | 255 | 345 | 13 | 89 | glycosyl hydrolase family 31 (GH31). GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 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. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AZN42907.1 | 1.26e-125 | 44 | 654 | 62 | 643 |
| AVM44715.1 | 5.39e-116 | 12 | 654 | 196 | 834 |
| QOY88337.1 | 4.26e-102 | 10 | 653 | 176 | 788 |
| CBK67651.1 | 4.02e-99 | 15 | 628 | 62 | 664 |
| QUT32038.1 | 4.02e-99 | 15 | 628 | 62 | 664 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2XN0_A | 8.62e-36 | 146 | 656 | 219 | 731 | 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 | 1.15e-35 | 146 | 656 | 219 | 731 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
| 4FNQ_A | 4.80e-22 | 153 | 616 | 222 | 690 | Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
| 3MI6_A | 4.93e-22 | 276 | 620 | 355 | 697 | 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] |
| 4FNR_A | 6.36e-22 | 153 | 616 | 222 | 690 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| G1UB44 | 4.72e-35 | 146 | 656 | 219 | 731 | Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1 |
| P43467 | 7.93e-26 | 153 | 593 | 224 | 668 | Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1 |
| Q9ALJ4 | 3.48e-21 | 153 | 616 | 222 | 690 | Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1 |
| Q92457 | 2.49e-16 | 129 | 507 | 214 | 591 | Alpha-galactosidase 2 OS=Hypocrea jecorina OX=51453 GN=agl2 PE=1 SV=1 |
| G4T4R7 | 5.10e-16 | 169 | 617 | 244 | 683 | Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000020 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |