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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s264_36V6.1 |
Family | GH31 |
Protein Properties | Length: 960 Molecular Weight: 108511 Isoelectric Point: 6.0214 |
Chromosome | Chromosome/Scaffold: 264 Start: 250580 End: 254412 |
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 | 300 | 794 | 0 |
FYFFAGPSPMGVVDEYTQLVGRPAAMPYWSFGFHQARYGYKDIEELESVLAKYDAINFPVESIWADIDHMDGYRDFTLHPEHFPEKRMRSFVQGLHLKNQ KLVMILDPGIKIDETYATFTRGRELGVYLRNGTGDGYYVTQVWPGATHIPDFLHPNALDWWTKEVEEFYKIVPFDGIWLDMNEPANFCSGPNCWFDPAVP CIIIDSCCMTCDNDPDKLTRWDNPPYKINGYKSKLPIYKNTVATSALHYDGTPVYNTHNVYGMAEGLATYKALEKVQKKRPFVLSRSSFVGGGAHSAHWT GDNGATWTDMKHSIASMLNSGLFGVPMVGVDLCGFYMETNEELCERWTQLGAFYPFARSHSDIHTGPQEIYLWKSVTETASKAFYWRYRLLPFFYTLMYE AHTSGAPIARPLFFEYWEDKETWEIDTQFLLGSSILVSPVLEPNQTSVRAYFPKGIWYNLFDTSDVIRAEDHGIWKHLSAPKDTINVHVRRGSIV |
Full Sequence |
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Protein Sequence Length: 960 Download |
MGAAIRKDQD CGKRPMSIES ASLRMLTGMA AVRVMMLLAL VLPTVSTIAD LSSGYRMTEI 60 NELADGSGVV AHLELTSGCE TYGPNLKELR LTARYEDGGR VHIHITDPLL PRWEIPDMLI 120 PRDRVEHIPI GQSTSPIRFT ETSYTLKRES NWIASHQLKI TWTKDPFSFS IIRRSNGDVL 180 FNTLPEAEGG RYAFNPMVFK DQYLEISTRL PQNSCLYGLG ESTRPSGMRL VPGQSYTLWA 240 TDIGSWNLDF PLYGSYPFLM DMRPDGQTHG VLFLNSNGMD IEYKSGDSLT FQVIGGVFDF 300 YFFAGPSPMG VVDEYTQLVG RPAAMPYWSF GFHQARYGYK DIEELESVLA KYDAINFPVE 360 SIWADIDHMD GYRDFTLHPE HFPEKRMRSF VQGLHLKNQK LVMILDPGIK IDETYATFTR 420 GRELGVYLRN GTGDGYYVTQ VWPGATHIPD FLHPNALDWW TKEVEEFYKI VPFDGIWLDM 480 NEPANFCSGP NCWFDPAVPC IIIDSCCMTC DNDPDKLTRW DNPPYKINGY KSKLPIYKNT 540 VATSALHYDG TPVYNTHNVY GMAEGLATYK ALEKVQKKRP FVLSRSSFVG GGAHSAHWTG 600 DNGATWTDMK HSIASMLNSG LFGVPMVGVD LCGFYMETNE ELCERWTQLG AFYPFARSHS 660 DIHTGPQEIY LWKSVTETAS KAFYWRYRLL PFFYTLMYEA HTSGAPIARP LFFEYWEDKE 720 TWEIDTQFLL GSSILVSPVL EPNQTSVRAY FPKGIWYNLF DTSDVIRAED HGIWKHLSAP 780 KDTINVHVRR GSIVPMQDFA MTTTLARKTP FSLLVAFAPS FHFAEFCAAG RSIVCRGIDR 840 EFATGQIYLD DDAQPTMDIT EGRASLVKLE AIRTYGHYVL RSTVTQPDCA INQRLIINTV 900 VVLGLQARPF SVHLNGRLAS VQVNANDSMM ELSGLNLFVR EAFELIWNIM PNGNGVHSR* 960 1020 |
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-78 | 320 | 486 | 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 | 9.0e-89 | 554 | 722 | 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 | 5.0e-105 | 320 | 704 | 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 | 6.0e-124 | 106 | 815 | 724 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 301 | 794 | 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 | 35 | 948 | 1 | 900 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001754376.1 | 0 | 57 | 948 | 1 | 861 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001765995.1 | 0 | 25 | 958 | 1 | 927 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001773000.1 | 0 | 40 | 947 | 25 | 923 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001779762.1 | 0 | 36 | 959 | 1 | 909 | 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 | 24 | 937 | 8 | 876 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
PDB | 3w37_A | 0 | 24 | 937 | 8 | 876 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
PDB | 3l4z_A | 0 | 59 | 947 | 55 | 868 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
PDB | 3l4y_A | 0 | 59 | 947 | 55 | 868 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
PDB | 3l4x_A | 0 | 59 | 947 | 55 | 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 |