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Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi2g10060.1 |
Family | GH31 |
Protein Properties | Length: 856 Molecular Weight: 95366.7 Isoelectric Point: 8.4422 |
Chromosome | Chromosome/Scaffold: 2 Start: 8259148 End: 8263282 |
Description | Glycosyl hydrolases family 31 protein |
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 | 358 | 839 | 0 |
LQGHSPTELITSYTGSTGRPPVLPRWITSGAVVGMQGGTDAVRRVWSQLRDHDVPVSAFWLQDWVGQRKTAIGSQLWWNWEVDDDHYAGWNDLVRDLRRG GVRTMTYCNPCLVPMGGKANARRHLFEEAKELGILVRDESGGPYMMPNTAFDVAMLDFTNPSACAWFKGILRGMAESGVSGWMADFGEGLPLDARLHSGE DPVAAHNRYPELWARVNREFADEWKKNSSGDHGTASEEEEEEEEGLVFFVRAGFRESSRWAMLFWEGDQMVSWQANDGIKSSVVGLLSGGLSGIPLNHSD AGGYCTVDLPPFLRYRRGEELLMRWMELNAFTVVFRTHEGNRPGSNAQFYSNARTLAHFARCAKVYKAWEFYRARLVKEAAETGLPVARHMFLYYPEDRR VQGMTCQQFLVGTELLVVPVLDKGRRTVAAYFPASDGASWRHVWTGQEFGNNGHGGVGAVHGFEAEVGAEVGYPAVFVRVGS |
Full Sequence |
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Protein Sequence Length: 856 Download |
MASPAHPKTT KKHNARLNNP FPRAVPAAAF RQYGDAAPPL SFAPSSAKLA QAHDHPVGSR 60 FRLRWDPSHG GAVSLAGIHV SSSVMWETIP GVAFVSAASA VTEADECRGS FALRDGRARL 120 VPDRQTVDRI RALYRCDADL LRAAAFQASE ETRFPVLLIT GVVSARKAGP ASSCCCGLRA 180 RIRAGQPIFS ARYWFLLEEK NNTQRNSGRK KKLSSGFPVR EEELSALLPR LKKEDEEEAR 240 APEEFNRVFL TYASERDERF YGFGEQFSRM EFKGKRVPVL VQEQGIGRGD QPITFAANLL 300 SYRSGGNWST TYAPSPFYMT SKMRSLYLEG YDYSIFDLTK PDRVQIQVYG NSVRGRILQG 360 HSPTELITSY TGSTGRPPVL PRWITSGAVV GMQGGTDAVR RVWSQLRDHD VPVSAFWLQD 420 WVGQRKTAIG SQLWWNWEVD DDHYAGWNDL VRDLRRGGVR TMTYCNPCLV PMGGKANARR 480 HLFEEAKELG ILVRDESGGP YMMPNTAFDV AMLDFTNPSA CAWFKGILRG MAESGVSGWM 540 ADFGEGLPLD ARLHSGEDPV AAHNRYPELW ARVNREFADE WKKNSSGDHG TASEEEEEEE 600 EGLVFFVRAG FRESSRWAML FWEGDQMVSW QANDGIKSSV VGLLSGGLSG IPLNHSDAGG 660 YCTVDLPPFL RYRRGEELLM RWMELNAFTV VFRTHEGNRP GSNAQFYSNA RTLAHFARCA 720 KVYKAWEFYR ARLVKEAAET GLPVARHMFL YYPEDRRVQG MTCQQFLVGT ELLVVPVLDK 780 GRRTVAAYFP ASDGASWRHV WTGQEFGNNG HGGVGAVHGF EAEVGAEVGY PAVFVRVGSP 840 VGERFVSNLR DLKVV* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06589 | GH31 | 1.0e-24 | 375 | 717 | 351 | + 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 | 2.0e-62 | 360 | 804 | 461 | + 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 | 1.0e-71 | 246 | 804 | 571 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
cd06594 | GH31_glucosidase_YihQ | 5.0e-146 | 375 | 717 | 344 | + YihQ is a bacterial alpha-glucosidase with a conserved glycosyl hydrolase family 31 (GH31) domain that catalyzes the release of an alpha-glucosyl residue from the non-reducing end of alpha-glucoside substrates such as alpha-glucosyl fluoride. Orthologs of YihQ that have not yet been functionally characterized are present in plants and fungi. YihQ has sequence similarity to other GH31 enzymes such as CtsZ, a 6-alpha-glucosyltransferase from Bacillus globisporus, and YicI, an alpha-xylosidase from Echerichia coli. In bacteria, YihQ (along with YihO) is important for bacterial O-antigen capsule assembly and translocation. | ||
PRK10426 | PRK10426 | 0 | 246 | 853 | 610 | + alpha-glucosidase; Provisional |
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 |
DDBJ | BAD81144.1 | 0 | 8 | 204 | 15 | 222 | alpha-glucosidase -like [Oryza sativa Japonica Group] |
DDBJ | BAD81144.1 | 0 | 244 | 855 | 315 | 932 | alpha-glucosidase -like [Oryza sativa Japonica Group] |
RefSeq | XP_002308887.1 | 0 | 8 | 855 | 5 | 875 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002455428.1 | 0 | 1 | 638 | 1 | 707 | hypothetical protein SORBIDRAFT_03g010640 [Sorghum bicolor] |
RefSeq | XP_002522166.1 | 0 | 8 | 855 | 5 | 874 | alpha-xylosidase, putative [Ricinus communis] |
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 | 1we5_F | 3e-27 | 258 | 806 | 160 | 644 | A Chain A, Crystal Structure Of Alpha-Xylosidase From Escherichia Coli |
PDB | 1we5_E | 3e-27 | 258 | 806 | 160 | 644 | A Chain A, Crystal Structure Of Alpha-Xylosidase From Escherichia Coli |
PDB | 1we5_D | 3e-27 | 258 | 806 | 160 | 644 | A Chain A, Crystal Structure Of Alpha-Xylosidase From Escherichia Coli |
PDB | 1we5_C | 3e-27 | 258 | 806 | 160 | 644 | A Chain A, Crystal Structure Of Alpha-Xylosidase From Escherichia Coli |
PDB | 1we5_B | 3e-27 | 258 | 806 | 160 | 644 | A Chain A, Crystal Structure Of Alpha-Xylosidase From Escherichia Coli |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CO467346 | 275 | 299 | 572 | 0 |
DR734448 | 252 | 292 | 543 | 0 |
EE184435 | 272 | 438 | 708 | 0 |
EE176645 | 269 | 441 | 708 | 0 |
EE290668 | 264 | 446 | 708 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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