| Basic Information | |
|---|---|
| Species | Eucalyptus grandis |
| Cazyme ID | Eucgr.K01950.1 |
| Family | GH31 |
| Protein Properties | Length: 657 Molecular Weight: 72363.4 Isoelectric Point: 6.2075 |
| Chromosome | Chromosome/Scaffold: 11 Start: 24865487 End: 24868644 |
| 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 | 54 | 501 | 0 |
| YFFPGPSPEEVMEQYTELIGRPTPMPYWSFGFHQCRWGYKNVPDLEGVVAGYAKANIPLEVMWTDIDHMDANKDFTLDPINFPVEKMKEFVSSLHENSQK YVLILDPGISVNKTYGTYIRGMQADIFLKREGVPYLGRVWPGPVYFPDFLHPSSESYWGGEIKRFHDVLPFDGLWIDMNELSNFNDPPPLPSALDNPPYK INNAGVHRPINNKTIPATSLHFGNISEYNAHNLYGLLEARATNKALVNVTGKRPFILSRSTFLSSGKHTAHWTGDNAATWDDLAYSVPAILNFGLFGIPM VGADICGFFWDTTEELCNRWIQSSISGDSVAASARKVLGLRYRLLPYLYTLMYEAYQKGIPIARPLFFSFPEDTMTYNINSQFLIGKGLMVTPVLKSGAQ TVDAYFPSGNWFDLFNYSNSVSTTSGMNVMLNAPPDHPHLHVREGNIL | |||
| Full Sequence |
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| Protein Sequence Length: 657 Download |
| MDVRSSVGSG GGGGGGVGAG TSHGVLLLNS NGMDVVYTGD RITYKVIGGV LDLYFFPGPS 60 PEEVMEQYTE LIGRPTPMPY WSFGFHQCRW GYKNVPDLEG VVAGYAKANI PLEVMWTDID 120 HMDANKDFTL DPINFPVEKM KEFVSSLHEN SQKYVLILDP GISVNKTYGT YIRGMQADIF 180 LKREGVPYLG RVWPGPVYFP DFLHPSSESY WGGEIKRFHD VLPFDGLWID MNELSNFNDP 240 PPLPSALDNP PYKINNAGVH RPINNKTIPA TSLHFGNISE YNAHNLYGLL EARATNKALV 300 NVTGKRPFIL SRSTFLSSGK HTAHWTGDNA ATWDDLAYSV PAILNFGLFG IPMVGADICG 360 FFWDTTEELC NRWIQSSISG DSVAASARKV LGLRYRLLPY LYTLMYEAYQ KGIPIARPLF 420 FSFPEDTMTY NINSQFLIGK GLMVTPVLKS GAQTVDAYFP SGNWFDLFNY SNSVSTTSGM 480 NVMLNAPPDH PHLHVREGNI LAMQGEAMTT EAARRTPFKL LVVVDGHGNS TGQVFLDDGD 540 DVEMGGEGNK WTLVKFYCEK TGNGVVVRSE VVNGEFALIE KWVIDKVTIL GLRKGTRMTK 600 LRGHELYNEV EAKSGQRTVT IAGKSSGGGE FVIAEVSGLS LLLGKTFKLE VKVPQS* 660 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd06600 | GH31_MGAM-like | 1.0e-86 | 73 | 375 | 305 | + 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 | 2.0e-92 | 73 | 375 | 308 | + 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. | ||
| COG1501 | COG1501 | 3.0e-93 | 44 | 530 | 512 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
| cd06602 | GH31_MGAM_SI_GAA | 5.0e-172 | 73 | 430 | 382 | + 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). | ||
| pfam01055 | Glyco_hydro_31 | 2.0e-177 | 54 | 501 | 471 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
| 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 | CBI39013.1 | 0 | 1 | 653 | 1101 | 1759 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI39013.1 | 0 | 15 | 640 | 216 | 859 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002317678.1 | 0 | 1 | 653 | 250 | 912 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317679.1 | 0 | 1 | 652 | 242 | 903 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002333838.1 | 0 | 1 | 653 | 233 | 895 | predicted protein [Populus trichocarpa] |
| 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 | 1 | 652 | 250 | 907 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3w37_A | 0 | 1 | 652 | 250 | 907 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3ctt_A | 0 | 18 | 650 | 226 | 867 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 2qmj_A | 0 | 18 | 650 | 226 | 867 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 2qly_A | 0 | 18 | 650 | 226 | 867 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO795307 | 673 | 37 | 653 | 0 |
| DY272797 | 300 | 65 | 363 | 0 |
| FC882813 | 285 | 65 | 348 | 0 |
| DR736759 | 330 | 48 | 377 | 0 |
| ES811873 | 268 | 93 | 359 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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