Species | Phocaeicola ilei | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola ilei | |||||||||||
CAZyme ID | MGYG000001750_01435 | |||||||||||
CAZy Family | GH31 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 7262; End: 9682 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH31 | 227 | 667 | 1.8e-112 | 0.9976580796252927 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1501 | YicI | 9.50e-144 | 77 | 726 | 94 | 730 | Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism]. |
pfam01055 | Glyco_hydro_31 | 5.44e-127 | 228 | 667 | 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 | 2.93e-83 | 247 | 560 | 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. |
PRK10658 | PRK10658 | 3.81e-66 | 48 | 664 | 63 | 665 | putative alpha-glucosidase; Provisional |
cd06593 | GH31_xylosidase_YicI | 8.28e-57 | 247 | 566 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ADY36155.1 | 0.0 | 1 | 806 | 1 | 802 |
QUT59614.1 | 0.0 | 17 | 805 | 17 | 793 |
QQY38322.1 | 0.0 | 17 | 805 | 17 | 793 |
QQY41700.1 | 0.0 | 17 | 805 | 17 | 793 |
ABR39486.1 | 0.0 | 17 | 805 | 17 | 793 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6JR6_A | 9.47e-102 | 24 | 806 | 36 | 837 | 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] |
6JR8_A | 1.35e-100 | 24 | 806 | 36 | 837 | Flavobacteriumjohnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101] |
5F7U_A | 6.28e-73 | 78 | 701 | 178 | 843 | Cycloalternan-formingenzyme from Listeria monocytogenes in complex with pentasaccharide substrate [Listeria monocytogenes EGD-e] |
5I0D_A | 7.07e-64 | 78 | 701 | 178 | 843 | Cycloalternan-formingenzyme from Listeria monocytogenes in complex with cycloalternan [Listeria monocytogenes EGD-e],5I0D_B Cycloalternan-forming enzyme from Listeria monocytogenes in complex with cycloalternan [Listeria monocytogenes EGD-e] |
4KMQ_A | 7.94e-64 | 78 | 701 | 199 | 864 | 1.9Angstrom resolution crystal structure of uncharacterized protein lmo2446 from Listeria monocytogenes EGD-e [Listeria monocytogenes EGD-e],4KWU_A 1.9 Angstrom resolution crystal structure of uncharacterized protein lmo2446 from Listeria monocytogenes EGD-e in complex with alpha-D-glucose, beta-D-glucose, magnesium and calcium [Listeria monocytogenes EGD-e],5HPO_A Cycloalternan-forming enzyme from Listeria monocytogenes in complex with maltopentaose [Listeria monocytogenes EGD-e],5HXM_A Cycloalternan-forming enzyme from Listeria monocytogenes in complex with panose [Listeria monocytogenes] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9F234 | 2.80e-85 | 23 | 740 | 30 | 747 | Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1 |
Q9P999 | 2.13e-69 | 185 | 726 | 152 | 681 | Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1 |
A7LXT0 | 9.39e-62 | 211 | 714 | 360 | 890 | Alpha-xylosidase BoGH31A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02646 PE=1 SV=1 |
P96793 | 1.51e-51 | 129 | 667 | 148 | 674 | Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1 |
Q5AW25 | 1.24e-49 | 139 | 686 | 178 | 715 | 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 |
---|---|---|---|---|---|
0.000249 | 0.999135 | 0.000182 | 0.000147 | 0.000140 | 0.000134 |
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