CAZyme Information: MGYG000001697_01974

Basic Information

• Species: Erysipelatoclostridium saccharogumia
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium saccharogumia
• CAZyme ID: MGYG000001697_01974
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
484		53109.84	4.2756

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001697	3141483	Isolate	Germany	Europe

• Gene Location: Start: 24592; End: 26046 Strand: +

Full Sequence      

MKLLKKVGLSALSLATAFSTVLSVQKGQIRAAEEFRGQLNSVDSVSVDGNVVNISYNNGA
VTGKITFLENGIFRYNVDPSGEFEEYAEVRKDIPGYESHTAKIQAQSDDSDKYSHPDANV
SDKGTVWEISTDEATIVLDKATAKMSIKNKSGDTIMSEAKSLVIGNQTIQSLDSKDDEYF
FGGGTQNGRFTHKGKSINIVNESSWTDGGVSSPNPFYWSTEGYGVLRNTFQDGKYDFGET
SAEVVATTHNESEFDAYYFVSNDADVNGKAETLLNEYYDVTGNPMLLPEYAFYLAHLNCY
NRDGWQESTSGNWVLEDGKTYRELGQASGYVIPEGTAAETLNNEAPSVEAENFKGTVNDD
TYKFSARAVIDGHVDNDMPLGWFLPNDGYGCGYGQNGYYQTRTSGEDTTRRDSVVDANVA
NLAKFTEYAEDHGVRSGLWTQAALTPDASEQDSRYNGFQNLRDFNKEVNVAGVSALKTDV
AWVG

Enzyme Prediction     

No EC number prediction in MGYG000001697_01974.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06596	GH31_CPE1046	8.22e-40	280	484	1	121	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.
cd14752	GH31_N	4.43e-18	168	282	10	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.
pfam16338	DUF4968	8.97e-09	50	158	1	90	Domain of unknown function (DUF4968). This family consists of uncharacterized proteins around 830 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as alpha-glucosidases, but the function of this protein is unknown.
COG1501	YicI	7.90e-08	129	317	106	280	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
PRK10658	PRK10658	2.73e-07	147	294	140	270	putative alpha-glucosidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM10857.1	1.01e-184	3	484	6	488
QOY60730.1	2.16e-154	37	484	50	501
BCT46261.1	3.02e-152	3	484	6	490
QUO30799.1	2.55e-140	25	484	12	472
BBK61154.1	8.28e-129	5	484	3	494

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6M76_A	1.49e-103	54	484	52	439	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]
7F7R_A	7.96e-103	54	484	52	439	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
7F7Q_A	2.17e-102	54	484	52	439	ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
5F7U_A	5.73e-06	120	385	180	459	Cycloalternan-formingenzyme from Listeria monocytogenes in complex with pentasaccharide substrate [Listeria monocytogenes EGD-e]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000400	0.998767	0.000266	0.000206	0.000175	0.000153

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001697_01974.