| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma15g14140.2 |
| Family | GH31 |
| Protein Properties | Length: 644 Molecular Weight: 71914.4 Isoelectric Point: 4.9311 |
| Chromosome | Chromosome/Scaffold: 15 Start: 10662230 End: 10666454 |
| 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 | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH31 | 22 | 489 | 0 |
| YFFSGSSPELVLEQYTELIGRPAPMPYWSFGFHQCRWGYKNVSDLEGVVDNYAKAGIPLEVMWTDIDYMDAYKDFTLDPINFPLDKMISFVDALHKNGQK YVLILDPGISVNKTDATYVRGLKADVYIKRNEVNYLGEVWPGPVYYPDFLNPRSQAFWGGEIKLFRDLLSFDGLWLDMNELSNFITSPPNPSSNLDNPPY KINNGEVQQSINYRTVPATSLHFGNITEYNAHNLYGLLESKVTNKALVDITGKRPFILSRSTFVSSGKYASHWTGDNAATWNDLAYSIPSILNSGIFGIP MVGADICGFGGNTTEELCRRWIQLGAFYPFARDHSEKNSIRQELYIWDSVASSARKVLGLRYSLLPYFYTLMYEAHTKGTPIARPLFFSFPEDVTTYKIN SQFLVGKGVLVSPVLQSGATTVNAYFPKGSWFDLFNVSNSVNAESGKYVTLDAPSDHINVHVGEGNIL | |||
| Full Sequence |
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| Protein Sequence Length: 644 Download |
| MDIVYGGDRI TYKVIGGVFD LYFFSGSSPE LVLEQYTELI GRPAPMPYWS FGFHQCRWGY 60 KNVSDLEGVV DNYAKAGIPL EVMWTDIDYM DAYKDFTLDP INFPLDKMIS FVDALHKNGQ 120 KYVLILDPGI SVNKTDATYV RGLKADVYIK RNEVNYLGEV WPGPVYYPDF LNPRSQAFWG 180 GEIKLFRDLL SFDGLWLDMN ELSNFITSPP NPSSNLDNPP YKINNGEVQQ SINYRTVPAT 240 SLHFGNITEY NAHNLYGLLE SKVTNKALVD ITGKRPFILS RSTFVSSGKY ASHWTGDNAA 300 TWNDLAYSIP SILNSGIFGI PMVGADICGF GGNTTEELCR RWIQLGAFYP FARDHSEKNS 360 IRQELYIWDS VASSARKVLG LRYSLLPYFY TLMYEAHTKG TPIARPLFFS FPEDVTTYKI 420 NSQFLVGKGV LVSPVLQSGA TTVNAYFPKG SWFDLFNVSN SVNAESGKYV TLDAPSDHIN 480 VHVGEGNILA LQGEAMTTDA ARKTAFQLVV VISSSRDSYG QVYLDDGEAL DIAGENDQWT 540 LVSFYGTLHN SSVIVTSKVT NGIFALDQRW IIDNIIFLGI PKYQRFNGMD LAGNELNIVK 600 GTDSMRTAVV KSESDSSSQF LNVQVSKLSL LIGEEFKLEI EIK* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd06600 | GH31_MGAM-like | 8.0e-108 | 41 | 400 | 363 | + This family includes the following closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), lysosomal acid alpha-glucosidase (GAA), neutral alpha-glucosidase C (GANC), the alpha subunit of neutral alpha-glucosidase AB (GANAB), and alpha-glucosidase II. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). 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. Alpha-glucosidase II is a 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. The MGAM-like family corresponds to subgroup 1 in the Ernst et al classification of GH31 enzymes. | ||
| COG1501 | COG1501 | 3.0e-119 | 12 | 574 | 579 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
| cd06604 | GH31_glucosidase_II_MalA | 1.0e-122 | 41 | 400 | 368 | + 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. | ||
| pfam01055 | Glyco_hydro_31 | 0 | 22 | 489 | 472 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
| cd06602 | GH31_MGAM_SI_GAA | 0 | 41 | 418 | 383 | + This family includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN66951.1 | 0 | 1 | 642 | 260 | 898 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI39013.1 | 0 | 1 | 629 | 234 | 859 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI39013.1 | 0 | 1 | 642 | 1128 | 1759 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002317679.1 | 0 | 1 | 641 | 269 | 903 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002333838.1 | 0 | 1 | 642 | 260 | 895 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3w38_A | 0 | 1 | 643 | 272 | 909 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
| PDB | 3w37_A | 0 | 1 | 643 | 272 | 909 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
| PDB | 3ctt_A | 0 | 10 | 639 | 251 | 867 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
| PDB | 2qmj_A | 0 | 10 | 639 | 251 | 867 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
| PDB | 2qly_A | 0 | 10 | 639 | 251 | 867 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO795307 | 662 | 5 | 638 | 0 |
| DY272797 | 322 | 33 | 353 | 0 |
| ES793134 | 288 | 199 | 486 | 0 |
| CO985275 | 231 | 414 | 644 | 0 |
| ES793134 | 62 | 487 | 546 | 0.0000001 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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