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CAZyme Information: MGYG000000250_00309
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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 | TF01-11 sp001414325 | |||||||||||
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| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; TF01-11; TF01-11 sp001414325 | |||||||||||
| CAZyme ID | MGYG000000250_00309 | |||||||||||
| CAZy Family | GH31 | |||||||||||
| CAZyme Description | Alpha-xylosidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 381109; End: 383472 Strand: + | |||||||||||
Full Sequence Download help
| MKVADGFWLS KKGYNVNYAS QAYKVETTEN SIKVLATPYT VMNRGMTLGG PNLEITYSST | 60 |
| SENIIKVHID HYRGGLDNSP RYELNEDTGY TPVIERTEDK VTLTSGDTRV EIKIGDDWDV | 120 |
| QFYYKDRHLT GGAWRATSII SESQFTANAR MNLQEDDEFF NYPQDAHTTY LREQLKTDIG | 180 |
| ECIYGFGEKF TPFVKNGQTV ETWNCDGGTC SDQSYKTVPF YISSKSYGVL VNSSDKVSFE | 240 |
| VNSDTVSKVT FTVPGEELEY FIIGGENLEH VLENYTTLTG KPALPPAYTF GLWLSTSFTT | 300 |
| SYDEKTVMSF IDGMKERKIP LQVFHFDCFW MKEYEWCNFE WDKDMFPDPK GLLDKLHNEK | 360 |
| GLEVCVWINS YIGQQSKLFD IGKEKGYFIK NLDGSVFQSD MWQPGMAIVD FTNPEACEWF | 420 |
| KGLLKKLFDM GVNNIKTDFG ERIPTKCKYY NGMDPIKMHN YYTYLYNKCV FEALEDYYGK | 480 |
| DKACLFARSA TVGGQKFPVH WGGDCYAEYS AMSETLRGGL SLCSSGFGFF SHDMGGFEAT | 540 |
| APADVYKRWC AFGLLSTHSR LHGSTSYRVP WVYDEDGDTE ACDVLRHYTV LKGRLMPYLW | 600 |
| AQANKTHNVG VPMMRSMIVA FSDDTACKYL DQQYMLGDNL CIVPVMNEEG IAEFYVPDCG | 660 |
| TWTDIQSGET YEGGKYYKRQ CDYFQTPILA RPNSIVTYGN FDAEDKMTVV YDYLEKADAV | 720 |
| IYGLEDGKSA TATIYDSESN KLTDIKAERN ANVITVSYNS TDKNFTVTAE GKTVEAKAGT | 780 |
| TSVEITL | 787 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH31 | 260 | 696 | 1.7e-117 | 0.9976580796252927 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG1501 | YicI | 0.0 | 8 | 776 | 1 | 762 | Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism]. |
| cd06593 | GH31_xylosidase_YicI | 0.0 | 280 | 595 | 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. |
| PRK10658 | PRK10658 | 0.0 | 1 | 693 | 1 | 665 | putative alpha-glucosidase; Provisional |
| pfam01055 | Glyco_hydro_31 | 3.10e-149 | 261 | 696 | 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 | 1.47e-77 | 280 | 589 | 1 | 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 |
|---|---|---|---|---|---|
| BAV13089.1 | 0.0 | 1 | 787 | 1 | 780 |
| ADL51183.1 | 0.0 | 1 | 787 | 1 | 780 |
| QAA31782.1 | 0.0 | 1 | 787 | 1 | 780 |
| CBL16634.1 | 0.0 | 1 | 787 | 1 | 778 |
| ADU21699.1 | 0.0 | 1 | 767 | 1 | 757 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2F2H_A | 3.99e-271 | 1 | 767 | 1 | 736 | 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] |
| 1XSI_A | 4.74e-271 | 1 | 767 | 1 | 736 | 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] |
| 1WE5_A | 9.74e-259 | 2 | 767 | 2 | 736 | 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 | 4.77e-97 | 181 | 696 | 202 | 715 | 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] |
| 5F7U_A | 1.20e-68 | 88 | 736 | 176 | 842 | Cycloalternan-formingenzyme from Listeria monocytogenes in complex with pentasaccharide substrate [Listeria monocytogenes EGD-e] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P31434 | 2.11e-270 | 1 | 767 | 1 | 736 | Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2 |
| Q5AW25 | 9.00e-235 | 1 | 695 | 1 | 695 | 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 | 1.06e-206 | 1 | 749 | 1 | 722 | Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1 |
| Q9F234 | 2.36e-60 | 178 | 771 | 144 | 743 | Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1 |
| Q9P999 | 1.19e-51 | 162 | 743 | 93 | 683 | 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 |
|---|---|---|---|---|---|
| 1.000075 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |