CAZyme Information: MGYG000000437_01133

Basic Information

• Species: Alistipes sp001941065
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp001941065
• CAZyme ID: MGYG000000437_01133
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
758	MGYG000000437_31|CGC1	85920.5	6.2166

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000437	3341375	MAG	Sweden	Europe

• Gene Location: Start: 14066; End: 16342 Strand: -

Full Sequence      

MAALAGLHLGVQAGELPAANPIVVGNTRVTVITPSLFRMEYAMQGRFVDDQTLFACDRSA
LCRDFTFSKVGPNRYQIETDYFRMQFEDDGYPAVGRYNMGLYLKKADGTETEIKGRANSG
KNLGGAISTLDMVKDRVSTQNGLLSREGWYVIDDTGKDLVIDGGLKLRDRTHVTDRYYFM
YGTDYKAAFASLGAVSGHVPMTRKYMHGMWYCRWWDYTADEYLQLIDDYDEHDFPIDNIV
FDMGWHLQKEATVGTGASLSRGWTGYTWNPRYIPDPEGLMRKMHERRLSVSINDHPHDGI
RPHEAGYADFLAEMRREKPESIINDSVVMFDLGDKTYMKYFFKYTHEPSERMGVDFWWLD
WQQSSTYPRVLGTTTSSLAWINKLYYDRSKRDGLRGASYSRWAGWGDHRYPIQFSGDSFA
NWNLLAFEVELTATSSNAGCYYWAHDIGGFYGGSGPEYPELYARWSQFGALSASLKIHCT
RDPKLDRRPWVQGEAATRSLRASYHLRSRLFPYIYTSVRQTHETMVPLIRQMYIDYPEAD
EAYENPQQYLFGDLLLVAPITTPGKGDNKIAAQTVWFPEGDTWYDWFSGKAYPGGQKPGV
AKGLDEFPLFARGGWIIPMQPYTPRPATEPLDELVLRCYPGADGADNTYTLYEDDGISDA
CDRGGYAKTALSYRREGSRVTIGIAAAEGSYEGQPRQRSYRIELPAVRSVGAVRVGPKRV
SPVRDETIRGYVLEIPARSIRTAVTVTVEQLQADGSGV

Enzyme Prediction     

No EC number prediction in MGYG000000437_01133.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH31	177	617	2.2e-104	0.9976580796252927

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06595	GH31_u1	7.16e-129	196	514	1	304	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	6.02e-95	178	617	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.
COG1501	YicI	5.87e-90	176	684	235	735	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06603	GH31_GANC_GANAB_alpha	1.67e-47	211	658	15	467	neutral alpha-glucosidase C, neutral alpha-glucosidase AB. This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.
cd06589	GH31	3.90e-46	197	501	1	262	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL08921.1	7.82e-308	10	748	15	744
BBL11713.1	7.82e-308	10	748	15	744
BBL00995.1	3.16e-307	10	748	15	744
AWI09084.1	4.38e-301	20	749	23	738
AGY54505.1	4.81e-300	20	713	39	721

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7WJ9_A	1.03e-108	20	660	33	650	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	1.52e-107	20	660	33	650	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]
7KMP_A	1.67e-46	177	729	408	967	ChainA, Alpha-xylosidase [Xanthomonas citri pv. citri str. 306],7KNC_A Chain A, Alpha-xylosidase [Xanthomonas citri pv. citri str. 306]
5X7O_A	9.56e-41	143	691	193	753	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]
5JOU_A	1.19e-40	177	702	377	924	Bacteroidesovatus Xyloglucan PUL GH31 [Bacteroides ovatus],5JOV_A Bacteroides ovatus Xyloglucan PUL GH31 with bound 5FIdoF [Bacteroides ovatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9P999	4.02e-43	177	688	192	690	Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
A7LXT0	6.52e-40	177	702	376	923	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
Q9FN05	5.18e-34	173	694	331	855	Probable glucan 1,3-alpha-glucosidase OS=Arabidopsis thaliana OX=3702 GN=PSL5 PE=1 SV=1
Q9BE70	8.07e-33	166	620	170	637	Neutral alpha-glucosidase C (Fragment) OS=Macaca fascicularis OX=9541 GN=GANC PE=2 SV=2
B9F676	1.15e-32	173	658	329	818	Probable glucan 1,3-alpha-glucosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os03g0216600 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.800196	0.199295	0.000132	0.000177	0.000102	0.000106

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000437_01133.