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CAZyme Information: EPrPAT00000017534-p1

You are here: Home > Sequence: EPrPAT00000017534-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Pythium aphanidermatum
Lineage Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
CAZyme ID EPrPAT00000017534-p1
CAZy Family GH17
CAZyme Description Alpha-glucosidase.
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
822 91065.89 6.6074
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444 12363 1223555 58 12305
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.20:35 3.2.1.177:14

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 331 688 1.3e-103 0.6838407494145199

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269888 GH31_MGAM_SI_GAA 8.36e-139 335 595 124 367
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase. This subgroup 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).
395838 Glyco_hydro_31 4.82e-136 324 688 133 442
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
269889 GH31_GANC_GANAB_alpha 2.96e-92 335 727 122 466
neutral alpha-glucosidase C, neutral alpha-glucosidase AB. This subgroup 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.
224418 YicI 2.33e-84 331 759 373 740
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
269890 GH31_glucosidase_II_MalA 7.45e-68 335 598 122 339
Alpha-glucosidase II-like. 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 subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.28e-144 174 726 57 789
2.10e-141 177 815 54 888
3.01e-140 170 781 51 852
8.08e-137 177 744 57 815
8.15e-134 178 806 61 891

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.76e-117 140 780 39 854
Sugar beet alpha-glucosidase with acarbose [Beta vulgaris],3W38_A Sugar beet alpha-glucosidase [Beta vulgaris],3WEL_A Sugar beet alpha-glucosidase with acarviosyl-maltotriose [Beta vulgaris],3WEM_A Sugar beet alpha-glucosidase with acarviosyl-maltotetraose [Beta vulgaris],3WEN_A Sugar beet alpha-glucosidase with acarviosyl-maltopentaose [Beta vulgaris],3WEO_A Sugar beet alpha-glucosidase with acarviosyl-maltohexaose [Beta vulgaris]
8.35e-96 335 806 403 857
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA [Homo sapiens],5NN5_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with 1-deoxynojirimycin [Homo sapiens],5NN6_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-hydroxyethyl-1-deoxynojirimycin [Homo sapiens],5NN8_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with acarbose [Homo sapiens]
8.35e-96 335 806 403 857
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-acetyl-cysteine [Homo sapiens]
8.68e-96 335 806 405 859
Crystal structure of human GAA [Homo sapiens],5KZX_A Crystal structure of human GAA [Homo sapiens]
3.57e-92 144 821 75 898
Crystal structure of the N-terminal domain of sucrase-isomaltase [Homo sapiens],3LPO_B Crystal structure of the N-terminal domain of sucrase-isomaltase [Homo sapiens],3LPO_C Crystal structure of the N-terminal domain of sucrase-isomaltase [Homo sapiens],3LPO_D Crystal structure of the N-terminal domain of sucrase-isomaltase [Homo sapiens],3LPP_A Crystal complex of N-terminal sucrase-isomaltase with kotalanol [Homo sapiens],3LPP_B Crystal complex of N-terminal sucrase-isomaltase with kotalanol [Homo sapiens],3LPP_C Crystal complex of N-terminal sucrase-isomaltase with kotalanol [Homo sapiens],3LPP_D Crystal complex of N-terminal sucrase-isomaltase with kotalanol [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.80e-125 133 779 25 827
Probable alpha-glucosidase Os06g0675700 OS=Oryza sativa subsp. japonica OX=39947 GN=Os06g0675700 PE=1 SV=1
6.87e-124 169 778 52 850
Alpha-xylosidase 1 OS=Arabidopsis thaliana OX=3702 GN=XYL1 PE=1 SV=1
2.95e-123 181 776 59 817
Alpha-glucosidase OS=Hordeum vulgare OX=4513 PE=2 SV=1
2.41e-119 132 778 26 848
Alpha-glucosidase OS=Spinacia oleracea OX=3562 PE=1 SV=1
2.08e-111 140 780 39 854
Alpha-glucosidase OS=Beta vulgaris OX=161934 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.493186 0.506807 CS pos: 25-26. Pr: 0.4733

TMHMM  Annotations      help

There is no transmembrane helices in EPrPAT00000017534-p1.