dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

CAG-617 sp000438115

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-617; CAG-617 sp000438115

CAZyme ID

MGYG000001771_00219

CAZy Family

GH31

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
407	MGYG000001771_8\|CGC1	46728.87	6.9978

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001771	1494481	MAG	Denmark	Europe

Gene Location

Start: 21798; End: 23021 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000001771_00219.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH31	195	378	2e-33	0.41217798594847777

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06595	GH31_u1	3.09e-67	214	389	1	170	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.
pfam01055	Glyco_hydro_31	4.32e-24	197	373	2	176	Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
COG1501	YicI	1.49e-19	69	376	96	415	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06589	GH31	2.20e-17	215	376	1	117	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.
cd06591	GH31_xylosidase_XylS	8.79e-12	215	373	1	153	xylosidase XylS-like. XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. 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 XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO26540.1	2.07e-217	40	388	10	358
QRP59757.1	1.43e-185	44	388	20	364
QQT79794.1	1.43e-185	44	388	20	364
ASM65107.1	1.95e-185	44	388	30	374
QUU06909.1	1.95e-185	44	388	30	374

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7WJ9_A	1.22e-54	47	376	39	364	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	1.22e-54	47	376	39	364	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]
6JR6_A	1.98e-08	192	313	235	343	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	1.98e-08	192	313	235	343	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]
3M46_A	1.21e-06	97	308	14	235	ChainA, Uncharacterized protein [Blautia obeum ATCC 29174],3M46_B Chain B, Uncharacterized protein [Blautia obeum ATCC 29174]