y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s80_200V6.1 |
Family | GH31 |
Protein Properties | Length: 939 Molecular Weight: 105640 Isoelectric Point: 5.4589 |
Chromosome | Chromosome/Scaffold: 80 Start: 1557151 End: 1560602 |
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 | 277 | 771 | 0 |
FYFFAGPSPMAVVDQYTRLVGRPAPMPYWSLGFHQSRYGYKDIGELETVMAKYEAINFPVESIWSDIDHMDGYRDFTLHPDHYPEERVRSFVKGLHERDQ KFVMIIDPGIKIDENYATFTRGRELGVYLKNGTGDGYYIAQVWPGFTHIPDFLHPNALDWWTKELEEFQKTVPYDGLWLDMNEPANFCGGSNCWYDPAVK CTIIDVCCMTCDNHPDVLTRWDNPPYAINGYANKLPIYKNTVAMTAEHYDGSRIYDTHNIYGMTEALATYNALKKISKKRPFVLSRSCFVGSGSHSAHWT GDNGATWTDMKYSIANLLNSGLFGVPMVGADICGFYFETNEELCQRWSQVGAFYPFARSHSDIHTGPQEIYLWKSVTETASNVFNWRYRLLPFFYTLLYE AHQSGAPVARPLFFEYPEDAETWTIDTQFLLGSSILVSPVLERGETSVHAYFPKGIWYNLFDTSKMIRAVDHGVWEHLPAPMDTINVHIRQGSII |
Full Sequence |
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Protein Sequence Length: 939 Download |
MLKVMALGWA LFLLTLVCSM VSATEDLNSA GYRVIEINEL ADGSGIAAHL KLISGCATYG 60 PDLEDLRLIA RYEEGGRVHV HITDAFRPRW EIPDSLIPRD RVQHVSVGQS TASIQVSESS 120 FTLAHESYAI SSHPLKIIWT KDPFSFAIIR RSNGEILFNT LPEAEGSPHA FNSMVFKDQY 180 LEISTRLPQN SYLYGLGEST SPDGMRLSQG RTYTLWATDI GSWNVDMPLY SMYPFVLDMR 240 KGGTAHGVLL LNSNGMDVEY KKGDSLTFRV IGGVFDFYFF AGPSPMAVVD QYTRLVGRPA 300 PMPYWSLGFH QSRYGYKDIG ELETVMAKYE AINFPVESIW SDIDHMDGYR DFTLHPDHYP 360 EERVRSFVKG LHERDQKFVM IIDPGIKIDE NYATFTRGRE LGVYLKNGTG DGYYIAQVWP 420 GFTHIPDFLH PNALDWWTKE LEEFQKTVPY DGLWLDMNEP ANFCGGSNCW YDPAVKCTII 480 DVCCMTCDNH PDVLTRWDNP PYAINGYANK LPIYKNTVAM TAEHYDGSRI YDTHNIYGMT 540 EALATYNALK KISKKRPFVL SRSCFVGSGS HSAHWTGDNG ATWTDMKYSI ANLLNSGLFG 600 VPMVGADICG FYFETNEELC QRWSQVGAFY PFARSHSDIH TGPQEIYLWK SVTETASNVF 660 NWRYRLLPFF YTLLYEAHQS GAPVARPLFF EYPEDAETWT IDTQFLLGSS ILVSPVLERG 720 ETSVHAYFPK GIWYNLFDTS KMIRAVDHGV WEHLPAPMDT INVHIRQGSI IPMQDFAMTT 780 TAARKTPFSL LVVFAPASDF AEFCAAPYSI VCQGSDREYA TGHIFLDDDI QPTMDITERR 840 ASHIKLEASR TDGHYVLRSI VTQPDYAIDQ GLVIKTVSVL GVQSQPFSVR VNGRLAAAHV 900 KVTASASLME ISELNLPLGE EFELIWNTMP NGSSSHSS* 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 | 5.0e-79 | 297 | 463 | 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 | 1.0e-94 | 531 | 699 | 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 | 4.0e-106 | 297 | 681 | 390 | + 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 | 4.0e-133 | 83 | 847 | 780 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 278 | 771 | 498 | + 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_001752856.1 | 0 | 10 | 938 | 2 | 909 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001756901.1 | 0 | 4 | 926 | 5 | 906 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001765995.1 | 0 | 1 | 938 | 1 | 928 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001773000.1 | 0 | 12 | 935 | 22 | 932 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001779762.1 | 0 | 13 | 937 | 2 | 908 | 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 | 12 | 924 | 20 | 904 | A Chain A, The Structure Of Endoglucanase From Termite, Nasutitermes Takasagoensis, At Ph 2.5. |
PDB | 3w37_A | 0 | 12 | 924 | 20 | 904 | A Chain A, The Structure Of Endoglucanase From Termite, Nasutitermes Takasagoensis, At Ph 2.5. |
PDB | 3ctt_A | 0 | 35 | 926 | 54 | 868 | A Chain A, The Structure Of Endoglucanase From Termite, Nasutitermes Takasagoensis, At Ph 2.5. |
PDB | 2qmj_A | 0 | 35 | 926 | 54 | 868 | A Chain A, The Structure Of Endoglucanase From Termite, Nasutitermes Takasagoensis, At Ph 2.5. |
PDB | 2qly_A | 0 | 35 | 926 | 54 | 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 |