y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s25_97V6.1 |
Family | GH31 |
Protein Properties | Length: 917 Molecular Weight: 102283 Isoelectric Point: 5.049 |
Chromosome | Chromosome/Scaffold: 25 Start: 697698 End: 701188 |
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 | 274 | 767 | 0 |
FYFFAGPAPLAVIDQYTNLIGRPTPMPYWSFGFHQCRWGYETIDEIKDVVANYKKANIPLDTIWNDIDYMDAYKDFTFDPVRYDENTVREFVKELHANGQ QYIVILDPGISVGYKNYSTLERGLKDDIFLKNEFGNNYLAQVWPGPVYFPDFLHPKASSWWTQEIADFFDKVPFDGLWIDMNEASNFCTGSACSFDTLTL GMGKNDSDNDRCLLHCVNGTSRFDDPPYKINHVGTYDNLGVKTIAMTVKHYNGVLEYDAHNLYGLCESIATQKTLRDVTGKRPFILSRSTFVGSGAHTAH WTGDNKATWEDLKYSIVSVINSGMFGVPMVGADICGFAGNTTEELCRRWMQLGAFYPFSRNHAALGTNSHEPYIWESVAEASRKALGLRYRLLPHLYTLM FEATKSGAPIARALFFSFPKDLNTLAINDQFLLGRSVLISPIVAEGLTSVNAYFPKGTWYNLFDFSKIVSTGERRMLPAPADSINVHVSEGQIL |
Full Sequence |
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Protein Sequence Length: 917 Download |
MAATIIAFAM ALLCFLNLTA ALSPKALRSF GAGHRMTSVF EFDDGSGFVA NLELITGTEI 60 YGPDISPLRM IARYDSDDRL HVHITDSIHA RWEVPQDIIP RPDSSSLVTH VKERDMEHSE 120 GLDPARNDRQ LQLSYTVEPF GFAITRTSTG ECLFNSTPPI RQDSGEPAFN SMVFKDQYLE 180 ISTQLPRNNS LFGIGESTRP DGLRLTRGRL YTLWATDIAA YKVDVDLYGA YPFYMDIREG 240 GATHGVLMLN SNGMDIWVGE DMLTYHVIGG VLDFYFFAGP APLAVIDQYT NLIGRPTPMP 300 YWSFGFHQCR WGYETIDEIK DVVANYKKAN IPLDTIWNDI DYMDAYKDFT FDPVRYDENT 360 VREFVKELHA NGQQYIVILD PGISVGYKNY STLERGLKDD IFLKNEFGNN YLAQVWPGPV 420 YFPDFLHPKA SSWWTQEIAD FFDKVPFDGL WIDMNEASNF CTGSACSFDT LTLGMGKNDS 480 DNDRCLLHCV NGTSRFDDPP YKINHVGTYD NLGVKTIAMT VKHYNGVLEY DAHNLYGLCE 540 SIATQKTLRD VTGKRPFILS RSTFVGSGAH TAHWTGDNKA TWEDLKYSIV SVINSGMFGV 600 PMVGADICGF AGNTTEELCR RWMQLGAFYP FSRNHAALGT NSHEPYIWES VAEASRKALG 660 LRYRLLPHLY TLMFEATKSG APIARALFFS FPKDLNTLAI NDQFLLGRSV LISPIVAEGL 720 TSVNAYFPKG TWYNLFDFSK IVSTGERRML PAPADSINVH VSEGQILPMQ EARLTSAEVK 780 KTPFTLVVVF SADASASASG KLFVDSGVDI EMGIQDGSST FVQFFAERSL HSGSLVSRVI 840 AGNYALEQGL VLQSIRFLGV SGPVSDVIVN GERIVSAEQL SYDARLESLQ VSGLSLLLGR 900 DFELRWAMKE LRWATQ* 960 |
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 | 8.0e-94 | 294 | 460 | 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). | ||
cd06602 | GH31_MGAM_SI_GAA | 1.0e-101 | 530 | 698 | 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). | ||
cd06604 | GH31_glucosidase_II_MalA | 1.0e-124 | 294 | 680 | 389 | + 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 | 5.0e-132 | 176 | 789 | 625 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 275 | 767 | 499 | + 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_001753937.1 | 0 | 31 | 908 | 6 | 873 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001754376.1 | 0 | 36 | 916 | 1 | 870 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001756901.1 | 0 | 1 | 916 | 1 | 916 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001766654.1 | 0 | 25 | 909 | 24 | 894 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769951.1 | 0 | 28 | 909 | 27 | 894 | 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 | 1 | 896 | 10 | 876 | A Chain A, Beta-Glycosidase From Pyrococcus Horikoshii |
PDB | 3w37_A | 0 | 1 | 896 | 10 | 876 | A Chain A, Beta-Glycosidase From Pyrococcus Horikoshii |
PDB | 3ctt_A | 0 | 46 | 907 | 63 | 869 | A Chain A, Beta-Glycosidase From Pyrococcus Horikoshii |
PDB | 2qmj_A | 0 | 46 | 907 | 63 | 869 | A Chain A, Beta-Glycosidase From Pyrococcus Horikoshii |
PDB | 2qly_A | 0 | 46 | 907 | 63 | 869 | 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 |