CAZyme Information: MGYG000003094_01448

Basic Information

• Species: Phocaeicola barnesiae
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola barnesiae
• CAZyme ID: MGYG000003094_01448
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
299	MGYG000003094_26|CGC1	33061.23	4.9883

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003094	3093382	MAG	Spain	Europe

• Gene Location: Start: 22441; End: 23340 Strand: +

Full Sequence      

MGVGAHLACLSGGSGRRGNRPVQSIQAAVGQQQPLVSEATLLNPTTVEVLFSNQQRMMLD
FYGENMVRFFQDNAGGIVRDPEAVPPAQILVDRPRLNPGTLQLEDEQGKITVRTPLIAVE
IDKQSGLFCIRDLASGKAVVEETAPVQFTGQQVTLTLKENPDEYFYGGGVQNGRFSHKGQ
AIEIVNTNQWTDGGVASPTPFYWSTRGYGMMGYTFAPGKYDFGASRPGTVLLTHDTSYLD
CFFWLDDTPVSLLNSFYQLTGHPVLLPKFGFYEGHLNAYNRDYWKEDAEKGILFEDGKK

Enzyme Prediction     

No EC number prediction in MGYG000003094_01448.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14752	GH31_N	1.04e-23	146	261	3	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.
COG1501	YicI	3.96e-13	97	282	90	279	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06596	GH31_CPE1046	2.53e-09	259	299	1	41	Clostridium CPE1046-like. CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. 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.
pfam13802	Gal_mutarotas_2	2.11e-06	162	221	1	67	Galactose mutarotase-like. This family is found N-terminal to glycosyl-hydrolase domains, and appears to be similar to the galactose mutarotase superfamily.
PRK10658	PRK10658	2.59e-06	161	271	157	268	putative alpha-glucosidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO24224.1	2.35e-126	27	299	32	303
QQA08685.1	2.58e-118	22	299	26	315
ALJ44641.1	2.58e-118	22	299	26	315
QCT77646.1	8.94e-118	29	299	41	310
CAH06794.1	8.94e-118	29	299	41	310

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6M76_A	3.58e-62	49	297	52	310	GH31alpha-N-acetylgalactosaminidase from Enterococcus faecalis [Enterococcus faecalis ATCC 10100],6M77_A GH31 alpha-N-acetylgalactosaminidase from Enterococcus faecalis in complex with N-acetylgalactosamine [Enterococcus faecalis ATCC 10100]
7F7Q_A	3.58e-62	49	297	52	310	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
7F7R_A	3.58e-62	49	297	52	310	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
5F7C_A	3.50e-08	151	290	190	333	Crystalstructure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_B Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_C Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_D Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000053	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003094_01448.