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CAZyme Information: MGYG000001395_00171
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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 | Listeria innocua | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Listeriaceae; Listeria; Listeria innocua | |||||||||||
| CAZyme ID | MGYG000001395_00171 | |||||||||||
| CAZy Family | GH31 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 72132; End: 75407 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH31 | 363 | 830 | 2.5e-121 | 0.9976580796252927 |
| CBM35 | 969 | 1087 | 3.3e-30 | 0.9747899159663865 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG1501 | YicI | 0.0 | 21 | 941 | 1 | 772 | Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism]. |
| cd06597 | GH31_transferase_CtsY | 1.52e-163 | 383 | 728 | 1 | 326 | CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like. CtsY is a bacterial 3-alpha-isomaltosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsZ. CtsY and CtsZ both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsZ belongs to a different subfamily. 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. |
| pfam01055 | Glyco_hydro_31 | 2.21e-125 | 364 | 830 | 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 | 1.91e-87 | 208 | 827 | 94 | 665 | putative alpha-glucosidase; Provisional |
| cd06589 | GH31 | 1.39e-77 | 383 | 723 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUR88128.1 | 0.0 | 1 | 1091 | 1 | 1091 |
| QGF43291.1 | 0.0 | 1 | 1091 | 1 | 1091 |
| CAC97767.1 | 0.0 | 1 | 1090 | 1 | 1090 |
| AGR04340.1 | 0.0 | 1 | 1091 | 1 | 1091 |
| AGR24844.1 | 0.0 | 1 | 1091 | 1 | 1091 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5F7U_A | 0.0 | 31 | 1091 | 3 | 1063 | Cycloalternan-formingenzyme from Listeria monocytogenes in complex with pentasaccharide substrate [Listeria monocytogenes EGD-e] |
| 4KMQ_A | 0.0 | 31 | 1091 | 24 | 1084 | 1.9Angstrom resolution crystal structure of uncharacterized protein lmo2446 from Listeria monocytogenes EGD-e [Listeria monocytogenes EGD-e],4KWU_A 1.9 Angstrom resolution crystal structure of uncharacterized protein lmo2446 from Listeria monocytogenes EGD-e in complex with alpha-D-glucose, beta-D-glucose, magnesium and calcium [Listeria monocytogenes EGD-e],5HPO_A Cycloalternan-forming enzyme from Listeria monocytogenes in complex with maltopentaose [Listeria monocytogenes EGD-e],5HXM_A Cycloalternan-forming enzyme from Listeria monocytogenes in complex with panose [Listeria monocytogenes] |
| 5I0D_A | 0.0 | 31 | 1091 | 3 | 1063 | Cycloalternan-formingenzyme from Listeria monocytogenes in complex with cycloalternan [Listeria monocytogenes EGD-e],5I0D_B Cycloalternan-forming enzyme from Listeria monocytogenes in complex with cycloalternan [Listeria monocytogenes EGD-e] |
| 5F7S_A | 7.71e-130 | 275 | 830 | 172 | 733 | Cycloalternan-degradingenzyme from Trueperella pyogenes [Trueperella pyogenes],5F7S_B Cycloalternan-degrading enzyme from Trueperella pyogenes [Trueperella pyogenes],5I0E_B Cycloalternan-degrading enzyme from Trueperella pyogenes in complex with isomaltose [Trueperella pyogenes],5I0F_B Cycloalternan-degrading enzyme from Trueperella pyogenes in complex with covalent intermediate [Trueperella pyogenes] |
| 5I0G_B | 1.12e-128 | 275 | 830 | 172 | 733 | Cycloalternan-degradingenzyme from Trueperella pyogenes in complex with cycloalternan [Trueperella pyogenes] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D2PPM7 | 4.33e-121 | 255 | 826 | 144 | 712 | 1,3-alpha-isomaltosidase OS=Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399) OX=479435 GN=Kfla_1895 PE=1 SV=1 |
| Q9P999 | 7.55e-62 | 267 | 871 | 103 | 656 | Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1 |
| P31434 | 2.57e-61 | 222 | 836 | 108 | 675 | Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2 |
| P96793 | 3.00e-61 | 221 | 912 | 105 | 748 | Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1 |
| Q5AW25 | 1.92e-59 | 156 | 854 | 75 | 716 | 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 SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.001633 | 0.578735 | 0.418085 | 0.000804 | 0.000416 | 0.000312 |
