You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000000014_02045
You are here: Home > Sequence: MGYG000000014_02045
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 | Clostridium butyricum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium butyricum | |||||||||||
| CAZyme ID | MGYG000000014_02045 | |||||||||||
| CAZy Family | GH31 | |||||||||||
| CAZyme Description | Alpha-xylosidase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 128247; End: 130592 Strand: + | |||||||||||
Full Sequence Download help
| MKFSNGCWLN KTGVQTFSPQ EIYSTKIEDD VLTLYAPCSK IYNRGCTLGG PVITYKISSP | 60 |
| MKNVIRVRAC HYMGTEAKTP GFEIYEKNDS NVLINEDEKN IVFQTGNLKM DFNKETVEMG | 120 |
| FFRGEQKLTS SKYRGMAYVK TEEEDFLDYP EKTYMREQLQ LSVGELVYGL GERFTPFVKN | 180 |
| GQTINIWNED GGTSTEQSYK SIPFYLTNKG YGVFVNHPEK VSFEVGSEKV TKVQFSVPGE | 240 |
| CLDYFIIGGD SMKEVIENYT SLTGKPAMPP AWSFGLWLST SFTTNYDEKT VNEFVNGMKD | 300 |
| RDIPLRVFHF DCFWMKDFNW CDFEWDKRVF PDPKGMLERL KSKDLNICVW INPYIAQESK | 360 |
| LFEEAKEGGY LLKRTNGDVW QWDMWQPGMA IVDFTNPDAC TWYSSKLKEL MAMGVDCFKT | 420 |
| DFGERIPTEG VKYFDGSDPY KMHNYYTQMY NNVVFNTIKE IKGEDEAVVF ARSATAGGQQ | 480 |
| FPVHWGGDCE SDYESMAESL RGGLSLCMSG FGFWSHDIGG FESTSTADVY KRWVAFGLLS | 540 |
| SHSRLHGSTS YRVPWAYDED ASEVVRFFSK LKCSIMPYLF KTADDANRIG IPVMRSMVME | 600 |
| YQDDDACTYL DKQYMLGDSI LVAPIFNDQG EAKYYLPEGK WTNFITGKKY DGGRWIKEYH | 660 |
| DYLSIPMMVK ENSLVAVGHD NTRPDYDFRE GVSVLAYDLA DKAEACTKVL DMKRNETLSV | 720 |
| TVLKDGNTIN VKSTGTDKSW SLVLKDVTNV ADVNGLTFEV VGNDTKITIP SGTCEVACKL | 780 |
| K | 781 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH31 | 244 | 674 | 1.4e-130 | 0.9953161592505855 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK10658 | PRK10658 | 0.0 | 1 | 672 | 1 | 665 | putative alpha-glucosidase; Provisional |
| cd06593 | GH31_xylosidase_YicI | 0.0 | 264 | 575 | 1 | 308 | alpha-xylosidase YicI-like. YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). 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. The YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes. |
| COG1501 | YicI | 0.0 | 8 | 766 | 1 | 760 | Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism]. |
| pfam01055 | Glyco_hydro_31 | 1.41e-176 | 245 | 675 | 1 | 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. |
| cd06589 | GH31 | 9.86e-80 | 264 | 568 | 1 | 264 | 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 |
|---|---|---|---|---|---|
| BBK78922.1 | 0.0 | 1 | 781 | 1 | 781 |
| QMW92847.1 | 0.0 | 1 | 781 | 1 | 781 |
| QCJ08483.1 | 0.0 | 1 | 781 | 1 | 781 |
| QJU46725.1 | 0.0 | 1 | 781 | 1 | 781 |
| QGH20124.1 | 0.0 | 1 | 781 | 1 | 781 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1XSI_A | 0.0 | 1 | 756 | 1 | 747 | Structureof a Family 31 alpha glycosidase [Escherichia coli],1XSI_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_A Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSK_A Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_B Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_C Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_D Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_E Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_F Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli] |
| 2F2H_A | 0.0 | 1 | 756 | 1 | 747 | Structureof the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_B Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_C Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_D Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_E Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_F Structure of the YicI thiosugar Michaelis complex [Escherichia coli] |
| 1WE5_A | 3.90e-307 | 2 | 756 | 2 | 747 | CrystalStructure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_B Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_C Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_D Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_E Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_F Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli] |
| 5F7C_A | 3.05e-123 | 151 | 677 | 184 | 717 | Crystalstructure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_B Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_C Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_D Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
| 6JR6_A | 2.40e-78 | 91 | 675 | 92 | 688 | Flavobacteriumjohnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR7_A Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P31434 | 0.0 | 1 | 756 | 1 | 747 | Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2 |
| Q5AW25 | 3.23e-257 | 1 | 730 | 1 | 751 | Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1 |
| P96793 | 1.08e-245 | 1 | 735 | 1 | 733 | Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1 |
| Q9F234 | 1.88e-69 | 168 | 678 | 150 | 677 | Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1 |
| Q9P999 | 3.10e-62 | 67 | 697 | 18 | 644 | Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS 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 |
|---|---|---|---|---|---|
| 1.000062 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |