y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 52272.m000013 |
Family | GH31 |
Protein Properties | Length: 311 Molecular Weight: 35995.4 Isoelectric Point: 6.9767 |
Chromosome | Chromosome/Scaffold: 52272 Start: 30 End: 962 |
Description | heteroglycan glucosidase 1 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 2 | 300 | 0 |
SKERYPTQQRLLEVARTFRREQFPLDYIVQDWQYWGSDKDGSWSGMTWDRERYPDPKAMTDEIHKLHMKLMVSIWPSIGDDTALAHELDQHHLRFAPLHW ISRHARVYDAYSPLGRQIYFKYIKSGLLDKGVDALWMDGTEVEVSSAMWNAMDNVRDTKALGSNAMGDFTRYLNPYTLLTTEGTYQGQRASDNKRVFTLT RSAWAGAQRTAAASWSGDIFANWTTFRQQISGGVNVTITGNPYWTQDTGGFFVTEFPGGEQNPAYRELYARWFQYAAFNPIMRVHGTSIEREPYLFKQL |
Full Sequence |
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Protein Sequence Length: 311 Download |
MSKERYPTQQ RLLEVARTFR REQFPLDYIV QDWQYWGSDK DGSWSGMTWD RERYPDPKAM 60 TDEIHKLHMK LMVSIWPSIG DDTALAHELD QHHLRFAPLH WISRHARVYD AYSPLGRQIY 120 FKYIKSGLLD KGVDALWMDG TEVEVSSAMW NAMDNVRDTK ALGSNAMGDF TRYLNPYTLL 180 TTEGTYQGQR ASDNKRVFTL TRSAWAGAQR TAAASWSGDI FANWTTFRQQ ISGGVNVTIT 240 GNPYWTQDTG GFFVTEFPGG EQNPAYRELY ARWFQYAAFN PIMRVHGTSI EREPYLFKQL 300 DPAVYQSMLN A 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06604 | GH31_glucosidase_II_MalA | 1.0e-34 | 6 | 297 | 316 | + Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This family also includes the MalA alpha-glucosidase from Sulfolobus sulfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source. | ||
cd06589 | GH31 | 3.0e-46 | 1 | 288 | 289 | + The enzymes of glycosyl hydrolase family 31 (GH31) 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. | ||
pfam01055 | Glyco_hydro_31 | 1.0e-64 | 1 | 297 | 312 | + 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 | COG1501 | 7.0e-65 | 1 | 297 | 307 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
cd06591 | GH31_xylosidase_XylS | 2.0e-136 | 1 | 308 | 315 | + XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. 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 XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002539422.1 | 0 | 1 | 311 | 1 | 311 | alpha-xylosidase, putative [Ricinus communis] |
RefSeq | YP_001684902.1 | 0 | 1 | 311 | 280 | 590 | glycoside hydrolase family protein [Caulobacter sp. K31] |
RefSeq | YP_001820101.1 | 0 | 1 | 311 | 299 | 608 | glycoside hydrolase family protein [Opitutus terrae PB90-1] |
RefSeq | ZP_04771455.1 | 0 | 1 | 311 | 280 | 590 | glycoside hydrolase family 31 [Asticcacaulis excentricus CB 48] |
RefSeq | ZP_05758490.1 | 0 | 2 | 299 | 213 | 511 | alpha-glycosidase [Bacteroides sp. D2] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2xvl_A | 0 | 2 | 309 | 440 | 763 | A Chain A, Crystal Structure Of Eutl Shell Protein Of The Bacterial Ethanolamine Micrompartment |
PDB | 2xvk_A | 0 | 2 | 309 | 440 | 763 | A Chain A, Crystal Structure Of Eutl Shell Protein Of The Bacterial Ethanolamine Micrompartment |
PDB | 2xvg_A | 0 | 2 | 309 | 440 | 763 | A Chain A, Crystal Structure Of Alpha-Xylosidase (Gh31) From Cellvibrio Japonicus |
PDB | 4ba0_A | 3e-20 | 2 | 310 | 269 | 565 | A Chain A, Crystal Structure Of Alpha-Xylosidase (Gh31) From Cellvibrio Japonicus |
PDB | 4b9z_A | 3e-20 | 2 | 310 | 269 | 565 | A Chain A, Crystal Structure Of Alpha-Xylosidase (Gh31) From Cellvibrio Japonicus |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO548297 | 252 | 54 | 298 | 6e-24 |
HO419407 | 111 | 186 | 295 | 6e-22 |
HO529785 | 148 | 189 | 308 | 3e-21 |
JG635864 | 259 | 6 | 252 | 1e-18 |
FR624153 | 178 | 128 | 299 | 5e-17 |
Sequence Alignments (This image is cropped. Click for full image.) |
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