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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s86_178V6.1 |
Family | GH31 |
Protein Properties | Length: 861 Molecular Weight: 95399.9 Isoelectric Point: 5.1594 |
Chromosome | Chromosome/Scaffold: 86 Start: 1226513 End: 1229841 |
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 | 211 | 697 | 0 |
FYFFVGPTPLDVVDQYTELVGRPAPMPYWSFGFHQCRWGYKNVDELKYVVENFKRASIPLDTIWNDIDYMQNYLDFTADPVNYPEEQLKDFVEELHANGQ HYVLILDPGISIAYENYTTLKRGLAEDIFLKDEQNENYLAQVWPGPVYFPDFFNPKGSAWWANEISEFHKKIPFDGLWIDMNEVSNFCSGTQCKFNGVVY PNLNECYLECKESSTQWDNPPYKITTAYKNIGDKTVAMGVKHFDGTLEYNAHNLYGLSESIATNKALQATRKKRPFILARSTFVGSGAQTAHWTGDNAAT FKDLEYSIATILNSGMVGVPMIGADICGFAGDSNMELCNRWMQLGAFYPFSRNHNIFGAIPQEPYVWDQVASSSRAALSMRYRLLPYFYSLMFEAHNKGA PIARPLFFAFPEDINTLKISTQFLLGSGVLVTPVVLPEATTVNGYFPMGTWYNLFDYASKVESKGEHFELAAPSDSINVHVHEGTIL |
Full Sequence |
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Protein Sequence Length: 861 Download |
MSSSLLLRIS DEVSVELVVE GQFRLHVQIS DKSNSRWEVP LSLVPRNDPS LRKGSRFALP 60 QEQLIKLTYT TKPFGFAVTR ISNDEVLFNS TPSVKTSLEG VESPSFNSMV FKDQYLEIST 120 HIPSSATLFG LGESTRPDGL PLVKGKTYSL WATDIGAMNA NVDLYGAYPY YIDVRAGGLT 180 HGVLLLNSNA MDIHYGGNFL TYRVIGGTFD FYFFVGPTPL DVVDQYTELV GRPAPMPYWS 240 FGFHQCRWGY KNVDELKYVV ENFKRASIPL DTIWNDIDYM QNYLDFTADP VNYPEEQLKD 300 FVEELHANGQ HYVLILDPGI SIAYENYTTL KRGLAEDIFL KDEQNENYLA QVWPGPVYFP 360 DFFNPKGSAW WANEISEFHK KIPFDGLWID MNEVSNFCSG TQCKFNGVVY PNLNECYLEC 420 KESSTQWDNP PYKITTAYKN IGDKTVAMGV KHFDGTLEYN AHNLYGLSES IATNKALQAT 480 RKKRPFILAR STFVGSGAQT AHWTGDNAAT FKDLEYSIAT ILNSGMVGVP MIGADICGFA 540 GDSNMELCNR WMQLGAFYPF SRNHNIFGAI PQEPYVWDQV ASSSRAALSM RYRLLPYFYS 600 LMFEAHNKGA PIARPLFFAF PEDINTLKIS TQFLLGSGVL VTPVVLPEAT TVNGYFPMGT 660 WYNLFDYASK VESKGEHFEL AAPSDSINVH VHEGTILPMQ ESALTSAEAM TTPFTLVVAF 720 PASKSSGFAT GKLFLDNGDD IEMVIRKGRS TFVRFFAQQS VQRGVLSSKV VSGDYAIQKG 780 LTVQTIIILG ANSAATSLTI NSVQVSSSIS SSFDSAAAST TISGLSVPVG SEFQLQWTTQ 840 AHSTSPQGLN LATVTCGEKL * 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 | 4.0e-96 | 231 | 397 | 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 | 459 | 627 | 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 | 3.0e-115 | 231 | 609 | 381 | + 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 | 2.0e-136 | 113 | 738 | 638 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 212 | 697 | 491 | + 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 | 11 | 837 | 41 | 871 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001754376.1 | 0 | 24 | 837 | 44 | 860 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001766654.1 | 0 | 12 | 860 | 66 | 914 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769951.1 | 0 | 12 | 844 | 66 | 898 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001779751.1 | 0 | 11 | 842 | 41 | 875 | 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 | 25 | 836 | 92 | 905 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 3w37_A | 0 | 25 | 836 | 92 | 905 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 3ctt_A | 0 | 24 | 837 | 96 | 868 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 2qmj_A | 0 | 24 | 837 | 96 | 868 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 2qly_A | 0 | 24 | 837 | 96 | 868 | 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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO795307 | 611 | 195 | 795 | 0 |
FC339838 | 264 | 479 | 742 | 0 |
FC422921 | 250 | 408 | 657 | 0 |
FC399720 | 255 | 490 | 744 | 0 |
FC422921 | 28 | 656 | 683 | 0.003 |
Sequence Alignments (This image is cropped. Click for full image.) |
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