CAZyme Information: MGYG000001306_02075

Basic Information

• Species: Phocaeicola coprocola
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola coprocola
• CAZyme ID: MGYG000001306_02075
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
258		28900.33	7.2882

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001306	4295617	Isolate	not provided	not provided

• Gene Location: Start: 2894; End: 3670 Strand: +

Full Sequence      

MSIHNDVSNSNMVNLKIVGVLGMLCFTGWLSAHNVKMEKEVIVGDGIAKFVPKGFNLSQM
PSFALKAEPQEKGMLPSNWQLYPIMEKKKGHASAYLDVPQGTSLYGGGEVTGPLLRNGQS
IKLWNTDSGAYSVDNGKRLYQSHPWVMGVRPDGTSFGILFDTPYKAKLTTTDERINFETE
GELFRIFVIDRESPQAVIKGLAELIGTMPMVPRWALGYQQCRFSYTPASRVIEVADTFRI
KRIPCDVIWMDIDYMDGY

Enzyme Prediction     

EC	3.2.1.20

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PLN02763	PLN02763	7.71e-58	62	258	34	230	hydrolase, hydrolyzing O-glycosyl compounds
COG1501	YicI	1.61e-32	93	258	144	310	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06604	GH31_glucosidase_II_MalA	1.59e-31	206	258	1	53	Alpha-glucosidase II-like. Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source.
pfam01055	Glyco_hydro_31	1.31e-28	187	258	1	72	Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd14752	GH31_N	1.01e-21	88	206	6	122	N-terminal domain of glycosyl hydrolase family 31 (GH31). This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). 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 of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT27192.1	1.05e-117	11	258	4	251
QUT41209.1	2.08e-117	31	258	24	251
SCV08112.1	8.26e-117	11	258	4	251
QUT78241.1	8.26e-117	11	258	4	251
QRQ55524.1	8.26e-117	11	258	4	251

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5DJW_A	7.03e-115	41	258	1	218	Crystalstructure of Family 31 alpha-glucosidase (BT_3299) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5DJW_B Crystal structure of Family 31 alpha-glucosidase (BT_3299) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
3W37_A	6.06e-25	75	258	179	364	Sugarbeet alpha-glucosidase with acarbose [Beta vulgaris],3W38_A Sugar beet alpha-glucosidase [Beta vulgaris],3WEL_A Sugar beet alpha-glucosidase with acarviosyl-maltotriose [Beta vulgaris],3WEM_A Sugar beet alpha-glucosidase with acarviosyl-maltotetraose [Beta vulgaris],3WEN_A Sugar beet alpha-glucosidase with acarviosyl-maltopentaose [Beta vulgaris],3WEO_A Sugar beet alpha-glucosidase with acarviosyl-maltohexaose [Beta vulgaris]
6JR6_A	1.92e-22	105	257	159	309	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	1.92e-22	105	257	159	309	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]
3TON_A	1.95e-17	104	256	180	333	CrystralStructure of the C-terminal Subunit of Human Maltase-Glucoamylase [Homo sapiens],3TON_B Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase [Homo sapiens],3TOP_A Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose [Homo sapiens],3TOP_B Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9F234	7.25e-33	84	258	122	304	Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
O04931	3.32e-24	75	258	179	364	Alpha-glucosidase OS=Beta vulgaris OX=161934 PE=1 SV=1
Q43763	3.76e-23	95	258	161	329	Alpha-glucosidase OS=Hordeum vulgare OX=4513 PE=2 SV=1
Q5AW25	2.43e-19	84	258	160	331	Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1
Q5AWI5	2.52e-19	98	256	156	319	Alpha/beta-glucosidase agdC OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdC PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.129059	0.843316	0.026474	0.000329	0.000351	0.000448

TMHMM  Annotations     

start	end
13	32