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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s65_69V6.1 |
Family | GH31 |
Protein Properties | Length: 401 Molecular Weight: 45909.7 Isoelectric Point: 8.6089 |
Chromosome | Chromosome/Scaffold: 65 Start: 298636 End: 301049 |
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 | 92 | 301 | 2.4e-39 |
NYKKVRNFVEELHANGQQYVLILNPGVSVAYKDYITLERGLKEDVFLKNKFEDNFLAQVWPDLVYFPDFLQPKVDSWWTTEMRDFFSMVPFDGLWIDMNK ASNFCSGNQCSFTPKSLAVFANKSNISNNECVLQCVERRKIGDKSILMTVKHWNDVLEYNAHILYGLSESVVTQRVLTTVTHKRPFVLSRSTFVGSGAHT AHWTGNNKVK |
Full Sequence |
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Protein Sequence Length: 401 Download |
MRHFAAQIFV PLVKSRAEIQ LQRKKNVMIN LKVVIGGVLD FYFFAEPTPL EVIDQYTKLV 60 DWLAPMPCWT FGTYQCRWGY DNIDDLKDVA QNYKKVRNFV EELHANGQQY VLILNPGVSV 120 AYKDYITLER GLKEDVFLKN KFEDNFLAQV WPDLVYFPDF LQPKVDSWWT TEMRDFFSMV 180 PFDGLWIDMN KASNFCSGNQ CSFTPKSLAV FANKSNISNN ECVLQCVERR KIGDKSILMT 240 VKHWNDVLEY NAHILYGLSE SVVTQRVLTT VTHKRPFVLS RSTFVGSGAH TAHWTGNNKV 300 KRTSFTLIVA FDKSSHATAF GKLFVDNCQD HEMEVRDGSS TFVQYFAKRS SHAGSLIERV 360 ISGDYALAQG LVLQNIKLLG VSKITHIIRL SFYLYSLSFN * 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02763 | PLN02763 | 2.0e-27 | 16 | 298 | 314 | + hydrolase, hydrolyzing O-glycosyl compounds | ||
COG1501 | COG1501 | 2.0e-27 | 33 | 298 | 299 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
cd06604 | GH31_glucosidase_II_MalA | 8.0e-35 | 65 | 299 | 270 | + 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 | 8.0e-62 | 42 | 300 | 290 | + 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-73 | 64 | 299 | 270 | + 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 | |
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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_001754376.1 | 0 | 34 | 300 | 219 | 534 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001754376.1 | 3e-32 | 299 | 382 | 732 | 815 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001756901.1 | 0 | 34 | 300 | 267 | 580 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001756901.1 | 1e-21 | 299 | 382 | 778 | 861 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001766654.1 | 0 | 34 | 335 | 258 | 601 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 34 | 301 | 285 | 572 | A Chain A, Crystal Structure Of Geranylgeranyl Pyrophosphate Synthase From Corynebacterium Glutamicum Atcc 13032 |
PDB | 3w38_A | 0.0005 | 300 | 387 | 772 | 857 | A Chain A, Crystal Structure Of Geranylgeranyl Pyrophosphate Synthase From Corynebacterium Glutamicum Atcc 13032 |
PDB | 3w37_A | 0 | 34 | 301 | 285 | 572 | A Chain A, Crystal Structure Of Geranylgeranyl Pyrophosphate Synthase From Corynebacterium Glutamicum Atcc 13032 |
PDB | 3w37_A | 0.0005 | 300 | 387 | 772 | 857 | A Chain A, Crystal Structure Of Geranylgeranyl Pyrophosphate Synthase From Corynebacterium Glutamicum Atcc 13032 |
PDB | 3l4z_A | 2e-39 | 34 | 298 | 255 | 543 | A Chain A, Crystal Structure Of Geranylgeranyl Pyrophosphate Synthase From Corynebacterium Glutamicum Atcc 13032 |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
BJ968861 | 231 | 86 | 299 | 0 |
HO795307 | 316 | 34 | 299 | 0 |
CN204532 | 199 | 95 | 276 | 0 |
FC431462 | 284 | 35 | 267 | 0 |
DR736759 | 309 | 39 | 311 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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