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CAZyme Information: MGYG000004523_01228

You are here: Home > Sequence: MGYG000004523_01228

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 Olsenella_E sp002160255
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Atopobiaceae; Olsenella_E; Olsenella_E sp002160255
CAZyme ID MGYG000004523_01228
CAZy Family GH31
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
527 57255.12 4.4753
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004523 1701429 MAG Israel Asia
Gene Location Start: 1207;  End: 2790  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004523_01228.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 72 320 1.5e-48 0.5386416861826698

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06596 GH31_CPE1046 1.37e-103 5 291 80 334
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.
COG1501 YicI 5.88e-44 35 375 386 710
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
pfam01055 Glyco_hydro_31 6.09e-43 71 320 210 442
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd06603 GH31_GANC_GANAB_alpha 4.84e-37 89 324 212 430
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.
cd06589 GH31 6.36e-24 10 195 71 265
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBK61154.1 2.24e-168 1 525 430 944
QUO30799.1 2.27e-167 3 525 409 916
QWT17625.1 7.61e-154 1 525 436 959
BCT46261.1 6.16e-150 3 525 427 918
QNM10857.1 1.01e-132 3 525 421 918

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6M76_A 1.69e-100 4 465 378 807
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 8.93e-100 4 465 378 807
ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
7F7Q_A 2.43e-99 4 465 378 807
ChainA, GH31 alpha-N-acetylgalactosaminidase [Enterococcus faecalis ATCC 10100]
7KBJ_A 5.66e-25 90 323 249 466
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 8.67e-25 90 323 509 726
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
Q9FN05 1.19e-26 82 378 558 824
Probable glucan 1,3-alpha-glucosidase OS=Arabidopsis thaliana OX=3702 GN=PSL5 PE=1 SV=1
Q14697 6.84e-26 90 323 596 813
Neutral alpha-glucosidase AB OS=Homo sapiens OX=9606 GN=GANAB PE=1 SV=3
Q4R4N7 9.13e-26 90 323 596 813
Neutral alpha-glucosidase AB OS=Macaca fascicularis OX=9541 GN=GANAB PE=2 SV=1
Q8BHN3 5.10e-24 90 323 596 813
Neutral alpha-glucosidase AB OS=Mus musculus OX=10090 GN=Ganab PE=1 SV=1
P79403 1.20e-23 90 323 596 813
Neutral alpha-glucosidase AB OS=Sus scrofa OX=9823 GN=GANAB 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
1.000059 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004523_01228.