logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001217_01449

You are here: Home > Sequence: MGYG000001217_01449

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 Firm-10 sp004552515
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-10; Firm-10 sp004552515
CAZyme ID MGYG000001217_01449
CAZy Family GH31
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
707 81488.86 4.9716
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001217 2504977 MAG Austria Europe
Gene Location Start: 883;  End: 3006  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001217_01449.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 202 598 8.1e-66 0.9953161592505855

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1501 YicI 1.71e-80 109 641 132 714
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
pfam01055 Glyco_hydro_31 2.14e-65 202 598 1 442
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
PRK10658 PRK10658 3.05e-44 118 576 153 647
putative alpha-glucosidase; Provisional
cd06592 GH31_NET37 1.01e-27 227 563 3 364
glucosidase NET37. NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. 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 3.89e-27 110 221 4 122
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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SCM56493.1 1.89e-173 4 695 44 769
QUT47628.1 3.82e-165 5 695 38 763
BCG53446.1 6.97e-165 4 693 37 758
BBD44713.1 7.60e-164 4 688 45 763
QNK57634.1 5.49e-123 115 704 108 687

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JR6_A 5.92e-49 122 688 152 781
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 6.54e-48 122 688 152 781
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]
2F2H_A 8.45e-37 36 576 60 648
Structureof the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_B Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_C Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_D Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_E Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_F Structure of the YicI thiosugar Michaelis complex [Escherichia coli]
1XSI_A 8.61e-37 36 576 60 648
Structureof a Family 31 alpha glycosidase [Escherichia coli],1XSI_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_A Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSK_A Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_B Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_C Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_D Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_E Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_F Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli]
5JOU_A 7.09e-35 198 680 374 924
Bacteroidesovatus Xyloglucan PUL GH31 [Bacteroides ovatus],5JOV_A Bacteroides ovatus Xyloglucan PUL GH31 with bound 5FIdoF [Bacteroides ovatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9P999 5.35e-49 122 678 108 702
Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
Q9F234 2.94e-42 122 694 143 767
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q5AW25 1.43e-38 109 600 163 698
Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1
P31434 4.61e-36 36 576 60 648
Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2
A7LXT0 3.88e-34 198 680 373 923
Alpha-xylosidase BoGH31A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02646 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000031 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001217_01449.