| Basic Information | |
|---|---|
| Species | Eucalyptus grandis |
| Cazyme ID | Eucgr.K01961.1 |
| Family | GH31 |
| Protein Properties | Length: 606 Molecular Weight: 67121 Isoelectric Point: 5.1938 |
| Chromosome | Chromosome/Scaffold: 11 Start: 25179474 End: 25182743 |
| Description | Glycosyl hydrolases family 31 protein |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH31 | 219 | 462 | 0 |
| YFFPGPSPEAVMEQYTELIGRLTPMPYWSFGFHQCQYGYKNVADLEGVVAGYAKANIPLEVMWTDIDYTDAYKDFTLDPINFPVEKMKEFVSSLHKTKYV LILDPGISVNGTYGTYIRGMQADIFIKHEGFPYLGDVWPGPVYFPDFLHPSSESYWGGEIKRFHDVLPFDGLWLDMNELSNFITSPPLPSILDNPPYKIN NLGVHRPINNNTTPATSYHFGNISDYDAHNLYGLLEARTINKAL | |||
| Full Sequence |
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| Protein Sequence Length: 606 Download |
| MGLLPASKRA VVFESESQTP TTAVPDDLIP HRPPSPPRRA LPEQTLTLLP LPPLFRSQCS 60 LSAASSDLVF VLRNTTPFSF TVSRRPSGDV LFDTSASDPS TFLVFKDQYL QLSSSLPPSR 120 SSLYSIGEHT KLSLRLQPNQ ILTLWNADIG SANLDVNLYG SHPFYMDVRS SVGGHGRHGR 180 GVGAGTSHGV LLLNSNDMDV VYSGDRITYK VIGGVLDLYF FPGPSPEAVM EQYTELIGRL 240 TPMPYWSFGF HQCQYGYKNV ADLEGVVAGY AKANIPLEVM WTDIDYTDAY KDFTLDPINF 300 PVEKMKEFVS SLHKTKYVLI LDPGISVNGT YGTYIRGMQA DIFIKHEGFP YLGDVWPGPV 360 YFPDFLHPSS ESYWGGEIKR FHDVLPFDGL WLDMNELSNF ITSPPLPSIL DNPPYKINNL 420 GVHRPINNNT TPATSYHFGN ISDYDAHNLY GLLEARTINK ALVNVTGAQT IDAYFPSGNW 480 FDLFNYSNSV STTLGMNVML NAPLDHPHLH VREGNILAMQ REAMTTEAAR TTAFKLLVVV 540 DGHGNSAGQM FLDDGDDVEM GGEGNKWTLV KFYCEKTENG VVVRSEVVNG EFALIEKWVI 600 DKVAI* 660 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01055 | Glyco_hydro_31 | 7.0e-7 | 467 | 517 | 52 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
| cd06600 | GH31_MGAM-like | 6.0e-43 | 244 | 400 | 160 | + 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. | ||
| cd06604 | GH31_glucosidase_II_MalA | 1.0e-53 | 238 | 456 | 225 | + 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 | 2.0e-81 | 219 | 469 | 253 | + 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 | 2.0e-89 | 238 | 467 | 236 | + 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 | 4 | 469 | 70 | 534 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002317679.1 | 0 | 15 | 469 | 99 | 543 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317679.1 | 3.9937e-43 | 466 | 605 | 706 | 845 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002534242.1 | 0 | 8 | 469 | 89 | 548 | alpha-glucosidase, putative [Ricinus communis] |
| RefSeq | XP_002534242.1 | 1.99993e-41 | 467 | 604 | 712 | 850 | alpha-glucosidase, 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 | 3w38_A | 0 | 50 | 469 | 132 | 546 | A Chain A, Crystral Structure Of The C-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3w38_A | 3.00018e-42 | 452 | 605 | 695 | 848 | A Chain A, Crystral Structure Of The C-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3w37_A | 0 | 50 | 469 | 132 | 546 | A Chain A, Crystral Structure Of The C-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3w37_A | 3.00018e-42 | 452 | 605 | 695 | 848 | A Chain A, Crystral Structure Of The C-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3ctt_A | 0 | 41 | 465 | 101 | 515 | A Chain A, Crystral Structure Of The C-Terminal Subunit Of Human Maltase- Glucoamylase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| DY265357 | 331 | 101 | 428 | 0 |
| FC915487 | 309 | 101 | 407 | 0 |
| DV025590 | 285 | 157 | 439 | 0 |
| CX545506 | 247 | 204 | 447 | 0 |
| JG572904 | 262 | 146 | 405 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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