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CAZyme Information: MGYG000003226_00934

You are here: Home > Sequence: MGYG000003226_00934

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 QALS01 sp900552625
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; QALS01; QALS01 sp900552625
CAZyme ID MGYG000003226_00934
CAZy Family GH31
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1486 161772.13 4.2625
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003226 3084338 MAG United States North America
Gene Location Start: 31547;  End: 36007  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003226_00934.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 334 573 1.5e-40 0.522248243559719

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01055 Glyco_hydro_31 2.93e-59 208 578 1 401
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 2.94e-53 201 847 230 744
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06595 GH31_u1 6.60e-47 227 522 1 302
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.
cd06589 GH31 2.98e-29 228 514 1 265
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.
cd06593 GH31_xylosidase_YicI 6.90e-27 228 520 1 308
alpha-xylosidase YicI-like. YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). 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. The YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AIE84875.1 1.69e-155 68 875 18 787
ARN57252.1 7.88e-141 66 922 30 862
AQQ09813.1 5.59e-138 66 922 30 862
QDV91404.1 1.28e-42 56 571 27 590
API87962.1 3.76e-42 63 569 21 545

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7WJ9_A 1.56e-39 71 575 41 561
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 1.51e-38 71 575 41 561
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]
5X7O_A 1.19e-27 70 610 47 673
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]
7KBJ_A 1.14e-21 198 572 8 413
ChainA, Neutral alpha-glucosidase AB Trypsin-cleaved Fragment #3 [Mus musculus],7KBJ_C Chain C, Neutral alpha-glucosidase AB Trypsin-cleaved Fragment #3 [Mus musculus],7KBR_A Chain A, Neutral alpha-glucosidase AB Trypsin-cleaved Fragment #3 [Mus musculus],7KBR_C Chain C, Neutral alpha-glucosidase AB Trypsin-cleaved Fragment #3 [Mus musculus],7L9E_A Chain A, Neutral alpha-glucosidase AB Trypsin-cleaved Fragment #3 [Mus musculus],7L9E_C Chain C, Neutral alpha-glucosidase AB Trypsin-cleaved Fragment #3 [Mus musculus]
5F0E_A 2.03e-21 198 572 268 673
Murineendoplasmic reticulum alpha-glucosidase II [Mus musculus],5H9O_A Complex of Murine endoplasmic reticulum alpha-glucosidase II with D-Glucose [Mus musculus],5H9O_C Complex of Murine endoplasmic reticulum alpha-glucosidase II with D-Glucose [Mus musculus],5HJO_A Murine endoplasmic reticulum alpha-glucosidase II with bound substrate analogue [Mus musculus],5HJO_C Murine endoplasmic reticulum alpha-glucosidase II with bound substrate analogue [Mus musculus],5HJR_A Murine endoplasmic reticulum alpha-glucosidase II with bound covalent intermediate [Mus musculus],5HJR_C Murine endoplasmic reticulum alpha-glucosidase II with bound covalent intermediate [Mus musculus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q5AW25 6.37e-22 165 573 207 644
Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1
Q14697 4.12e-21 183 572 340 760
Neutral alpha-glucosidase AB OS=Homo sapiens OX=9606 GN=GANAB PE=1 SV=3
Q9P999 6.85e-21 187 569 172 570
Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
Q8BHN3 1.22e-20 198 572 355 760
Neutral alpha-glucosidase AB OS=Mus musculus OX=10090 GN=Ganab PE=1 SV=1
Q4R4N7 2.77e-20 183 572 340 760
Neutral alpha-glucosidase AB OS=Macaca fascicularis OX=9541 GN=GANAB PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000002 1.000053 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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