logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004019_00393

You are here: Home > Sequence: MGYG000004019_00393

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 Bacteroides massiliensis_A
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides massiliensis_A
CAZyme ID MGYG000004019_00393
CAZy Family GH31
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
710 MGYG000004019_3|CGC1 80868.74 6.5169
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004019 3250001 MAG United Kingdom Europe
Gene Location Start: 41437;  End: 43569  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 170 601 5.1e-88 0.9953161592505855

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01055 Glyco_hydro_31 8.81e-92 170 601 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.
COG1501 YicI 5.21e-83 51 667 139 737
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06592 GH31_NET37 5.30e-80 193 567 1 364
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.
cd06603 GH31_GANC_GANAB_alpha 8.89e-33 189 640 1 467
neutral alpha-glucosidase C, neutral alpha-glucosidase AB. This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.
PRK10658 PRK10658 2.99e-30 51 598 143 665
putative alpha-glucosidase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALJ58469.1 0.0 1 687 27 713
QUT90418.1 0.0 1 687 27 713
QDO71138.1 0.0 1 687 27 713
AXY72919.1 0.0 1 687 30 714
AEW01609.1 0.0 3 687 31 713

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4XPO_A 0.0 3 687 36 719
Crystalstructure of a novel alpha-galactosidase from Pedobacter saltans [Pseudopedobacter saltans],4XPP_A Crystal structure of Pedobacter saltans GH31 alpha-galactosidase complexed with D-galactose [Pseudopedobacter saltans],4XPQ_A Crystal structure of Pedobacter saltans GH31 alpha-galactosidase complexed with L-fucose [Pseudopedobacter saltans]
4XPR_A 0.0 3 687 36 719
Crystalstructure of the mutant D365A of Pedobacter saltans GH31 alpha-galactosidase [Pseudopedobacter saltans],4XPS_A Crystal structure of the mutant D365A of Pedobacter saltans GH31 alpha-galactosidase complexed with p-nitrophenyl-alpha-galactopyranoside [Pseudopedobacter saltans]
2F2H_A 1.32e-41 48 603 138 671
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 1.35e-41 48 603 138 671
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]
6JR6_A 1.40e-39 6 648 89 737
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9F234 3.22e-45 61 659 143 732
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
Q9P999 2.57e-43 99 683 148 702
Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
P31434 7.17e-41 48 603 138 671
Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2
P96793 3.32e-37 58 601 151 674
Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1
Q5AW25 2.60e-31 51 640 164 734
Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD 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
1.000049 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004019_00393.