Species | Parabacteroides sp003480915 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp003480915 | |||||||||||
CAZyme ID | MGYG000003701_01914 | |||||||||||
CAZy Family | GH31 | |||||||||||
CAZyme Description | Alpha-xylosidase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 419918; End: 421519 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH31 | 144 | 530 | 1.1e-87 | 0.9110070257611241 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06592 | GH31_NET37 | 1.53e-173 | 139 | 503 | 1 | 364 | glucosidase NET37. NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. 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 | 7.80e-61 | 67 | 531 | 191 | 665 | Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism]. |
pfam01055 | Glyco_hydro_31 | 6.95e-60 | 153 | 527 | 40 | 433 | Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. |
cd06593 | GH31_xylosidase_YicI | 7.10e-35 | 143 | 434 | 11 | 304 | 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. |
cd06597 | GH31_transferase_CtsY | 7.65e-35 | 146 | 436 | 14 | 325 | CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like. CtsY is a bacterial 3-alpha-isomaltosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsZ. CtsY and CtsZ both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsZ belongs to a different subfamily. 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT50281.1 | 0.0 | 4 | 533 | 3 | 531 |
QCQ32141.1 | 8.02e-270 | 4 | 532 | 3 | 527 |
QCQ36424.1 | 1.14e-269 | 4 | 532 | 3 | 527 |
QKH84612.1 | 2.29e-269 | 4 | 532 | 3 | 527 |
QCQ51611.1 | 2.29e-269 | 4 | 532 | 3 | 527 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2F2H_A | 3.78e-34 | 68 | 503 | 195 | 635 | 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 | 3.82e-34 | 68 | 503 | 195 | 635 | 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] |
5F7C_A | 1.88e-29 | 95 | 527 | 270 | 706 | 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] |
1WE5_A | 1.09e-28 | 68 | 503 | 195 | 635 | 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] |
5F7S_A | 1.40e-26 | 107 | 532 | 262 | 729 | Cycloalternan-degradingenzyme from Trueperella pyogenes [Trueperella pyogenes],5F7S_B Cycloalternan-degrading enzyme from Trueperella pyogenes [Trueperella pyogenes],5I0E_B Cycloalternan-degrading enzyme from Trueperella pyogenes in complex with isomaltose [Trueperella pyogenes],5I0F_B Cycloalternan-degrading enzyme from Trueperella pyogenes in complex with covalent intermediate [Trueperella pyogenes] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q69ZQ1 | 5.74e-57 | 108 | 524 | 282 | 705 | Myogenesis-regulating glycosidase OS=Mus musculus OX=10090 GN=Myorg PE=1 SV=2 |
Q6NSJ0 | 1.01e-55 | 108 | 524 | 283 | 703 | Myogenesis-regulating glycosidase OS=Homo sapiens OX=9606 GN=MYORG PE=1 SV=2 |
P31434 | 2.06e-33 | 68 | 503 | 195 | 635 | Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2 |
P96793 | 7.71e-29 | 23 | 518 | 164 | 653 | Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1 |
Q5AW25 | 1.47e-25 | 35 | 527 | 177 | 687 | Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000963 | 0.515692 | 0.482664 | 0.000246 | 0.000215 | 0.000210 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.