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CAZyme Information: MGYG000004358_00100
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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; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; | |||||||||||
| CAZyme ID | MGYG000004358_00100 | |||||||||||
| CAZy Family | GH31 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 22228; End: 28659 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH31 | 491 | 744 | 7.6e-50 | 0.5386416861826698 |
| CBM32 | 1067 | 1184 | 1.8e-16 | 0.8870967741935484 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd06596 | GH31_CPE1046 | 5.58e-147 | 276 | 715 | 1 | 334 | Clostridium CPE1046-like. CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. Enzymes of the GH31 family possess a wide range of different 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. |
| COG1501 | YicI | 9.04e-54 | 73 | 792 | 62 | 710 | Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism]. |
| pfam01055 | Glyco_hydro_31 | 8.81e-48 | 428 | 744 | 159 | 442 | Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. |
| cd08759 | Type_III_cohesin_like | 1.62e-36 | 1271 | 1438 | 1 | 167 | Cohesin domain, interaction partner of dockerin. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. Two specific calcium-dependent interactions between cohesin and dockerin appear to be essential for cellulosome assembly, type I and type II. This subfamily represents type III cohesins and closely related domains. |
| cd06589 | GH31 | 1.86e-35 | 363 | 614 | 21 | 265 | 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 |
|---|---|---|---|---|---|
| QWT17625.1 | 0.0 | 17 | 2067 | 21 | 2112 |
| QNM10857.1 | 0.0 | 46 | 2063 | 50 | 2019 |
| BCT46261.1 | 0.0 | 46 | 2060 | 49 | 2041 |
| BBK61154.1 | 0.0 | 38 | 2066 | 39 | 2075 |
| QUO30799.1 | 0.0 | 49 | 1393 | 35 | 1367 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6M76_A | 1.72e-237 | 42 | 1054 | 32 | 963 | GH31alpha-N-acetylgalactosaminidase from Enterococcus faecalis [Enterococcus faecalis ATCC 10100],6M77_A GH31 alpha-N-acetylgalactosaminidase from Enterococcus faecalis in complex with N-acetylgalactosamine [Enterococcus faecalis ATCC 10100] |
| 7F7R_A | 9.17e-237 | 42 | 1054 | 32 | 963 | ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100] |
| 7F7Q_A | 2.50e-236 | 42 | 1054 | 32 | 963 | ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100] |
| 4LPL_A | 3.01e-20 | 1033 | 1188 | 23 | 182 | Structureof CBM32-1 from a family 31 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens ATCC 13124] |
| 2XVG_A | 3.91e-19 | 502 | 805 | 629 | 934 | crystalstructure of alpha-xylosidase (GH31) from Cellvibrio japonicus [Cellvibrio japonicus],2XVK_A crystal structure of alpha-xylosidase (GH31) from Cellvibrio japonicus in complex with 5-fluoro-alpha-D-xylopyranosyl fluoride [Cellvibrio japonicus],2XVL_A crystal structure of alpha-xylosidase (GH31) from Cellvibrio japonicus in complex with Pentaerythritol propoxylate (5 4 PO OH) [Cellvibrio japonicus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9F234 | 4.14e-21 | 65 | 792 | 48 | 714 | Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1 |
| Q9FN05 | 1.31e-19 | 509 | 745 | 566 | 780 | Probable glucan 1,3-alpha-glucosidase OS=Arabidopsis thaliana OX=3702 GN=PSL5 PE=1 SV=1 |
| B9F676 | 1.98e-18 | 497 | 745 | 551 | 778 | Probable glucan 1,3-alpha-glucosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os03g0216600 PE=3 SV=1 |
| P38138 | 3.55e-16 | 490 | 746 | 570 | 811 | Glucosidase 2 subunit alpha OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ROT2 PE=1 SV=1 |
| P79403 | 2.35e-15 | 504 | 747 | 591 | 813 | Neutral alpha-glucosidase AB OS=Sus scrofa OX=9823 GN=GANAB PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000462 | 0.998574 | 0.000235 | 0.000261 | 0.000230 | 0.000192 |
