y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s157_63V6.1 |
Family | GH31 |
Protein Properties | Length: 946 Molecular Weight: 106528 Isoelectric Point: 6.0362 |
Chromosome | Chromosome/Scaffold: 157 Start: 449412 End: 452993 |
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 | 296 | 783 | 0 |
YFFAGPSPRKVLDQYTLFVGRPAPMPFWTLGFHQSRYGYKTLKEVETVVAKYKEIGLPLESMWSDIDYMDRFRDFTIDPDTYPPVEFRKFVDTLHANNQK FTMIVDPGIKVEDSYPPYVRGKELDIFLKTESGEEYLGQVWPGAVHYPDFLHPKAKQWWTKEISEFYKVMPFDGLWLDMNEPSNFCSGPNCYYPPDVVCP EALDWCCMVCDNTNVSRWDRPPYRITNTWNKELYEKTVTMTARHYNDVKHYDAHNIYGFSQTVATFKALKEVTKKRPFVMSRSLYPGSGASAAHWSGDNG ASWNDLRYSIASILNSGLFGIPMVGADICGFIPATWEELCNRWIQVGAFYPFARDHSDVHFGPQELYLWKSVTHSARKVLPLRYKLLPFMYTLLHEAHMT GAPVARALFFVFPEDPTTYDVSDQFLLGDAILVSPVVSEGQTSVNAYIPKGNWWNLFNWSPIHSNGSYYKLDAPWDTINVHVRSGFIL |
Full Sequence |
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Protein Sequence Length: 946 Download |
MAFVRKFPVT TLLVNLCLLL LFSFVTLRSP STVAENQVGY GYRVICVNQV MNGDALIADL 60 DLIKRTDVYG PDIERLQLTV RYDNQDRIRV HITDANTLRW EVPPDLIPRA TSQELKSLRN 120 TTYSPDSSKA ACRNLRLPEI QNPTIPLQNP DHPLEFSYTT EIFGFAITRR SNGEVLFNST 180 PSVSTANGLS NNLVFKDQYI ELSTQLPKDA ALFGLGEGTH SSGLRLAKGN TYTLWATDIG 240 SYRTDIDLYG SYPIYIDVRK GGLAHGVQLV NSNGMDCVYG EDGLTFKMIG GVLDLYFFAG 300 PSPRKVLDQY TLFVGRPAPM PFWTLGFHQS RYGYKTLKEV ETVVAKYKEI GLPLESMWSD 360 IDYMDRFRDF TIDPDTYPPV EFRKFVDTLH ANNQKFTMIV DPGIKVEDSY PPYVRGKELD 420 IFLKTESGEE YLGQVWPGAV HYPDFLHPKA KQWWTKEISE FYKVMPFDGL WLDMNEPSNF 480 CSGPNCYYPP DVVCPEALDW CCMVCDNTNV SRWDRPPYRI TNTWNKELYE KTVTMTARHY 540 NDVKHYDAHN IYGFSQTVAT FKALKEVTKK RPFVMSRSLY PGSGASAAHW SGDNGASWND 600 LRYSIASILN SGLFGIPMVG ADICGFIPAT WEELCNRWIQ VGAFYPFARD HSDVHFGPQE 660 LYLWKSVTHS ARKVLPLRYK LLPFMYTLLH EAHMTGAPVA RALFFVFPED PTTYDVSDQF 720 LLGDAILVSP VVSEGQTSVN AYIPKGNWWN LFNWSPIHSN GSYYKLDAPW DTINVHVRSG 780 FILPMQEYAN TTALVRSSPV TLLVVFSGVE QESASGELFL DDDTEIGMEI RPKTSTHIKF 840 VAAKSASRGS VRSTVRYGEW AEQQGLYVHK IVLVGLMTPA SSLLIDGAPS PDIVTLNFDK 900 ASSIQEISGL RLSAGKDFEV AWTSTTHAVD SIATSLWQLS CLHSN* 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 | 9.0e-90 | 315 | 480 | 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). | ||
cd06603 | GH31_GANC_GANAB_alpha | 3.0e-101 | 315 | 696 | 389 | + This family includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae. | ||
cd06604 | GH31_glucosidase_II_MalA | 5.0e-118 | 315 | 696 | 387 | + 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-142 | 145 | 848 | 715 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 296 | 783 | 494 | + 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 | 19 | 922 | 1 | 899 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001756901.1 | 0 | 9 | 922 | 3 | 906 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001765995.1 | 0 | 21 | 931 | 11 | 925 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001773000.1 | 0 | 1 | 945 | 1 | 946 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001779762.1 | 0 | 25 | 922 | 5 | 897 | 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 | 6 | 876 | 8 | 851 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
PDB | 3w37_A | 0 | 6 | 876 | 8 | 851 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
PDB | 3ctt_A | 0 | 48 | 922 | 57 | 868 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
PDB | 2qmj_A | 0 | 48 | 922 | 57 | 868 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
PDB | 2qly_A | 0 | 48 | 922 | 57 | 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 |