y
Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.008G120000.1 |
Family | GH31 |
Protein Properties | Length: 932 Molecular Weight: 103669 Isoelectric Point: 6.5944 |
Chromosome | Chromosome/Scaffold: 08 Start: 7759295 End: 7764808 |
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 | 275 | 767 | 0 |
FYFFSGPSPLAVVDQYTALIGRPAPMPYWAFGFHQCRWGYHNLSVVEDVVENYKKAQIPLDVIWNDDDHMDGHKDFTLNLVNYPRPKLLAFLEKIHSIGM KYIVIIDPGIGVNSSYGVYQRGIANDVFIKYEGEPYLAQVWPGAVNFPDFLNPKTVDWWGDEVRRFHELVPVDGLWIDMNEASNFCSGLCKIPKGKQCPS GTGPGWVCCLDCKNITKTRWDDPPYKINASGLQVPIGYKTIATSAVHYNGVLEYDAHSLYGFSQAIATHKALQGLEGKRPFILSRSTYVGSGKYAAHWTG DNKGTWEDLKYSISTMINFGIFGVPMVGSDICGFYPAPTEELCNRWIEVGAFYPFSRDHANFYSPRQELYQWDSVAESARNALGMRYKILPYLYTLSYEA HTTGAPIARPLFFSFPDYTECYGLSTQFLLGSSLMISPVLEQGKSQVKALFPPGSWYNLFDMTQAITSEGGQYVTLDAPLHVVNVHLHQNTIL |
Full Sequence |
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Protein Sequence Length: 932 Download |
MFSSTGSFFS LFFFSFLLVL LLSFYQVNSS STPTKIGKGY RLISIEETPD GGIVGILQVK 60 QNNKIYGPDI PLLQLYVKHE TQDRLRVHIT DAEKQRWEVP YNLLPREKAQ ALKQTIGRSR 120 KNPITVQEYS GSELIFSYIA DPFSFAVKRK SNGQTLFNSS SDGSGSFGEM VFKDQYLEIS 180 TQLPKDASLY GLGENTQPHG IKLYPGVPYT LYTTDISAIN LNADLYGSHP VYMDLRKVKG 240 QAYAHAVLLL NSNGMDVFYR GTSLTYKIIG GVFDFYFFSG PSPLAVVDQY TALIGRPAPM 300 PYWAFGFHQC RWGYHNLSVV EDVVENYKKA QIPLDVIWND DDHMDGHKDF TLNLVNYPRP 360 KLLAFLEKIH SIGMKYIVII DPGIGVNSSY GVYQRGIAND VFIKYEGEPY LAQVWPGAVN 420 FPDFLNPKTV DWWGDEVRRF HELVPVDGLW IDMNEASNFC SGLCKIPKGK QCPSGTGPGW 480 VCCLDCKNIT KTRWDDPPYK INASGLQVPI GYKTIATSAV HYNGVLEYDA HSLYGFSQAI 540 ATHKALQGLE GKRPFILSRS TYVGSGKYAA HWTGDNKGTW EDLKYSISTM INFGIFGVPM 600 VGSDICGFYP APTEELCNRW IEVGAFYPFS RDHANFYSPR QELYQWDSVA ESARNALGMR 660 YKILPYLYTL SYEAHTTGAP IARPLFFSFP DYTECYGLST QFLLGSSLMI SPVLEQGKSQ 720 VKALFPPGSW YNLFDMTQAI TSEGGQYVTL DAPLHVVNVH LHQNTILPMQ QGGMISKEAR 780 MTPFALVVTF PAGASDGKAA GKLFLDDDEL PEMKLASGSA TYVDFYATVS QGTVKLWSEV 840 QESKFALDKG WKISKVAVLG LGRSGAPSAL EFDGKPVTAA SNIELTSLEQ KYLEDLQVGS 900 EKKSSVMVEV NGLEIPVGKN FAMSWKMGIS G* 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 | 2.0e-87 | 295 | 459 | 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 | 2.0e-93 | 528 | 696 | 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). | ||
cd06603 | GH31_GANC_GANAB_alpha | 3.0e-94 | 295 | 678 | 393 | + 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 | 2.0e-122 | 295 | 678 | 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. | ||
pfam01055 | Glyco_hydro_31 | 0 | 276 | 767 | 496 | + 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 |
EMBL | CAA10382.2 | 0 | 28 | 929 | 33 | 935 | alpha-D-xylosidase [Tropaeolum majus] |
RefSeq | XP_002282429.1 | 0 | 14 | 931 | 5 | 924 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002311455.1 | 0 | 27 | 931 | 6 | 910 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315944.1 | 0 | 7 | 931 | 3 | 928 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531635.1 | 0 | 1 | 931 | 1 | 930 | alpha-glucosidase, putative [Ricinus communis] |
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 | 15 | 863 | 13 | 853 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 3w37_A | 0 | 15 | 863 | 13 | 853 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 3lpp_D | 0 | 65 | 925 | 105 | 898 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 3lpp_C | 0 | 65 | 925 | 105 | 898 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 3lpp_B | 0 | 65 | 925 | 105 | 898 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |