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CAZyme Information: EPrPVT00000023287-p1

You are here: Home > Sequence: EPrPVT00000023287-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 Phytopythium vexans
Lineage Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
CAZyme ID EPrPVT00000023287-p1
CAZy Family GT48
CAZyme Description Alpha-glucosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
507 57192.39 5.9971
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PvexansDAOMBR484 11991 1223560 34 11957
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 232 492 1.8e-66 0.5058548009367682

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269888 GH31_MGAM_SI_GAA 6.60e-119 251 491 1 246
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 4.34e-86 233 491 2 232
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
269890 GH31_glucosidase_II_MalA 2.75e-70 251 491 1 215
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.
224418 YicI 1.21e-56 29 491 43 459
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
269889 GH31_GANC_GANAB_alpha 8.77e-45 251 491 1 221
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.82e-130 11 491 27 538
2.17e-128 17 491 37 518
2.21e-128 15 491 31 527
2.21e-128 15 491 31 527
2.25e-128 15 491 39 544

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.14e-126 15 491 42 548
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]
3.71e-95 12 496 75 556
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]
6.51e-94 16 491 54 516
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-acetyl-cysteine [Homo sapiens]
6.51e-94 16 491 54 516
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]
6.76e-94 16 491 56 518
Crystal structure of human GAA [Homo sapiens],5KZX_A Crystal structure of human GAA [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.04e-122 15 491 42 548
Alpha-glucosidase OS=Beta vulgaris OX=161934 PE=1 SV=1
8.98e-121 17 491 34 520
Probable alpha-glucosidase Os06g0675700 OS=Oryza sativa subsp. japonica OX=39947 GN=Os06g0675700 PE=1 SV=1
1.27e-115 15 491 32 543
Alpha-xylosidase 1 OS=Arabidopsis thaliana OX=3702 GN=XYL1 PE=1 SV=1
1.17e-114 23 491 38 514
Alpha-glucosidase OS=Hordeum vulgare OX=4513 PE=2 SV=1
3.52e-111 13 491 35 544
Alpha-glucosidase OS=Spinacia oleracea OX=3562 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000032 0.000003

TMHMM  Annotations      help

There is no transmembrane helices in EPrPVT00000023287-p1.