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CAZyme Information: MGYG000004325_00303

You are here: Home > Sequence: MGYG000004325_00303

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella;
CAZyme ID MGYG000004325_00303
CAZy Family CBM32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
356 38781.24 10.0458
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004325 2029971 MAG Israel Asia
Gene Location Start: 29433;  End: 30503  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004325_00303.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14752 GH31_N 1.68e-20 164 278 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.
COG1501 YicI 7.25e-10 73 299 62 279
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
pfam16338 DUF4968 4.55e-09 52 143 1 79
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.
cd06596 GH31_CPE1046 1.17e-07 276 301 1 26
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.
PRK10658 PRK10658 5.20e-07 111 290 89 270
putative alpha-glucosidase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QOY60730.1 9.31e-116 32 301 46 315
QWT17625.1 1.03e-100 17 301 21 312
QNM10857.1 1.08e-94 46 302 50 307
BCT46261.1 3.45e-87 46 301 49 304
QUO30799.1 2.95e-86 49 301 35 287

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6M76_A 1.47e-70 42 301 32 294
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 1.47e-70 42 301 32 294
ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
7F7R_A 1.47e-70 42 301 32 294
ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000460 0.998593 0.000237 0.000257 0.000226 0.000187

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004325_00303.