y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s43_19V6.1 |
Family | GH31 |
Protein Properties | Length: 897 Molecular Weight: 101588 Isoelectric Point: 6.3909 |
Chromosome | Chromosome/Scaffold: 43 Start: 142345 End: 145756 |
Description | alpha-xylosidase 1 |
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 | 267 | 756 | 0 |
FYFFLGPSPLDVVDQFTQLVGRPAPQPYWSFGFHQCRWGYRNVSMTKAVVENFRKAKIPLDTMWNDIDYMDKYKDFTNDKERFPLEEWRAFVDELHANGQ QYVIIIDPGISIAYQNYGTYIRGLEANIYLKKQNGENYLGQVWPGPVFFPDFFHPNATQWWINETQSFYNQIPFDGMWIDMNELANFCTGISCTWNGTII DDYTSCYLQCPNVLNHTKYDIPTYKINHEGTYEGLGYRTAAMTVKHYDGTIEYNVHNLYGLSEAIATNKAMTIVREKRPFVLSRSGFIGSGAHTAHWTGD NGASFNDLAYSIVTVLNFGIFGIPMIGADICGFNDETTEDICNRWIQVGAFHPFSRAHNNIANKPKELYLWESVTISAQKALGLRYRLLPFFYTLNYEAN KKGYPIVRPLFFAFPTDPNTLNVNYQFLIGNSILVSPVVTANTTSIEAYFPKGTWYNMFDWSKIQSVGENFTLSAPWDSINVHIHEGVIL |
Full Sequence |
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Protein Sequence Length: 897 Download |
MASGKIFFSA LVLFVISVKL PEVDAGIKFN EAFMDRQRGM HILTSMKEYE NKQGFEATLG 60 FVSESGNDTY GEDINPLQVT VRIEKKTRLR VYISDYSNSR WEVPHSLLPR PKLSSKLKHV 120 SSPQLAVTYT RKPFGFAVTR ISNGEVLFNS TPPTTGNKNL LFNSLVFKDQ YLELSTQLPS 180 TAALFGLGES TRPDGLKLNK NRTFTLWATD TGSIRTDVDL YGSYPFYLDG REGGLFHGVL 240 LLNSNGMEVV YQENYLTYKV LGGVLDFYFF LGPSPLDVVD QFTQLVGRPA PQPYWSFGFH 300 QCRWGYRNVS MTKAVVENFR KAKIPLDTMW NDIDYMDKYK DFTNDKERFP LEEWRAFVDE 360 LHANGQQYVI IIDPGISIAY QNYGTYIRGL EANIYLKKQN GENYLGQVWP GPVFFPDFFH 420 PNATQWWINE TQSFYNQIPF DGMWIDMNEL ANFCTGISCT WNGTIIDDYT SCYLQCPNVL 480 NHTKYDIPTY KINHEGTYEG LGYRTAAMTV KHYDGTIEYN VHNLYGLSEA IATNKAMTIV 540 REKRPFVLSR SGFIGSGAHT AHWTGDNGAS FNDLAYSIVT VLNFGIFGIP MIGADICGFN 600 DETTEDICNR WIQVGAFHPF SRAHNNIANK PKELYLWESV TISAQKALGL RYRLLPFFYT 660 LNYEANKKGY PIVRPLFFAF PTDPNTLNVN YQFLIGNSIL VSPVVTANTT SIEAYFPKGT 720 WYNMFDWSKI QSVGENFTLS APWDSINVHI HEGVILPLQE SALTSIEVRK TPFTLVVVFP 780 SGALSGKANG YVFLDNGDEI IIYLKVNKSS LIIFEASLKN GEGVLKSKLK FKEYALEEGW 840 ILDGVILLGI NTTHTSFYFN KNSINPERKI LGEEGLHISG LNYPLGEAFE LKWNST* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06602 | GH31_MGAM_SI_GAA | 7.0e-92 | 519 | 687 | 170 | + 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). | ||
cd06602 | GH31_MGAM_SI_GAA | 5.0e-97 | 287 | 453 | 169 | + 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). | ||
cd06604 | GH31_glucosidase_II_MalA | 6.0e-105 | 287 | 669 | 385 | + 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 | 1.0e-126 | 169 | 813 | 662 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 268 | 756 | 495 | + 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 | |
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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 | 43 | 895 | 1 | 862 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001760562.1 | 0 | 40 | 896 | 1 | 857 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001766654.1 | 0 | 28 | 895 | 24 | 893 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769951.1 | 0 | 41 | 895 | 33 | 893 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001778793.1 | 0 | 9 | 894 | 13 | 891 | 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 | 70 | 850 | 73 | 851 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 3w37_A | 0 | 70 | 850 | 73 | 851 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 3ctt_A | 0 | 54 | 798 | 64 | 774 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 2qmj_A | 0 | 54 | 798 | 64 | 774 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 2qly_A | 0 | 54 | 798 | 64 | 774 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |