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CAZyme Information: MGYG000000733_00171

You are here: Home > Sequence: MGYG000000733_00171

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; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; Borkfalkia;
CAZyme ID MGYG000000733_00171
CAZy Family GH31
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
752 83544.61 4.5103
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000733 1893651 MAG Kazakhstan Asia
Gene Location Start: 44452;  End: 46710  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000733_00171.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 333 576 4.4e-42 0.5269320843091335

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01055 Glyco_hydro_31 2.16e-59 203 571 1 390
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd06595 GH31_u1 1.30e-50 222 525 1 302
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup. This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. 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 2.83e-44 142 571 173 618
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06589 GH31 1.53e-30 223 517 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.
cd06593 GH31_xylosidase_YicI 7.02e-27 223 523 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ARN57252.1 1.11e-117 139 580 249 664
AQQ09813.1 2.43e-115 139 580 249 664
AIE84875.1 5.15e-108 60 605 15 527
AHF12332.1 3.15e-43 49 586 23 599
BCJ40002.1 9.23e-43 52 582 34 591

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7WJ9_A 3.32e-39 60 574 35 557
ChainA, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJA_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJB_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363]
7WJC_A 3.38e-38 60 574 35 557
ChainA, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJD_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJE_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJF_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363]
6JR8_A 4.97e-23 129 583 163 650
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]
6JR6_A 6.56e-23 129 583 163 650
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]
5X7O_A 6.59e-20 65 572 47 627
Crystalstructure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase [Paenibacillus sp. 598K],5X7O_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase [Paenibacillus sp. 598K],5X7P_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with acarbose [Paenibacillus sp. 598K],5X7P_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with acarbose [Paenibacillus sp. 598K],5X7Q_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with maltohexaose [Paenibacillus sp. 598K],5X7Q_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with maltohexaose [Paenibacillus sp. 598K],5X7R_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with isomaltohexaose [Paenibacillus sp. 598K],5X7R_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with isomaltohexaose [Paenibacillus sp. 598K],5X7S_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative [Paenibacillus sp. 598K],5X7S_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative [Paenibacillus sp. 598K]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9F234 3.34e-22 199 577 229 628
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q9P999 1.49e-20 182 573 172 571
Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
Q5AW25 5.92e-19 203 572 257 638
Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1
B3PEE6 3.90e-17 202 579 233 627
Oligosaccharide 4-alpha-D-glucosyltransferase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agd31B PE=1 SV=1
Q8BHN3 2.04e-15 193 575 355 760
Neutral alpha-glucosidase AB OS=Mus musculus OX=10090 GN=Ganab PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000005 1.000034 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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