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CAZyme Information: PITG_10846-t26_1-p1

You are here: Home > Sequence: PITG_10846-t26_1-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 Phytophthora infestans
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora infestans
CAZyme ID PITG_10846-t26_1-p1
CAZy Family GH35
CAZyme Description lysosomal alpha-glucosidase, putative
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1149 125620.34 6.2475
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PinfestansT30-4 19344 403677 1547 17797
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.20:38 3.2.1.10:16 3.2.1.48:16

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 378 913 5.8e-127 0.9953161592505855

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395838 Glyco_hydro_31 1.46e-158 378 913 1 442
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
269888 GH31_MGAM_SI_GAA 5.97e-126 397 820 1 367
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).
224418 YicI 1.72e-108 249 956 124 709
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
269889 GH31_GANC_GANAB_alpha 2.57e-100 397 956 1 467
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.
269890 GH31_glucosidase_II_MalA 1.35e-74 397 823 1 339
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
0.0 1 1149 1 1223
9.62e-247 29 1066 12 977
1.72e-219 23 909 10 837
7.16e-159 37 987 27 830
8.37e-151 86 994 72 893

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.38e-147 119 1064 25 867
Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase [Homo sapiens],2QMJ_A Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose [Homo sapiens],3CTT_A Crystal complex of N-terminal Human Maltase-Glucoamylase with Casuarine [Homo sapiens]
8.45e-147 119 1064 25 867
Crystal complex of N-terminal Human Maltase-Glucoamylase with BJ2661 [Homo sapiens],3L4U_A Crystal complex of N-terminal Human Maltase-Glucoamylase with de-O-sulfonated kotalanol [Homo sapiens],3L4V_A Crystal complex of N-terminal Human Maltase-Glucoamylase with kotalanol [Homo sapiens],3L4W_A Crystal complex of N-terminal Human Maltase-Glucoamylase with miglitol [Homo sapiens],3L4X_A Crystal complex of N-terminal Human Maltase-Glucoamylase with NR4-8 [Homo sapiens],3L4Y_A Crystal complex of N-terminal Human Maltase-Glucoamylase with NR4-8II [Homo sapiens],3L4Z_A Crystal complex of N-terminal Human Maltase-Glucoamylase with Salacinol [Homo sapiens]
4.18e-146 36 976 1 804
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-acetyl-cysteine [Homo sapiens]
4.18e-146 36 976 1 804
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]
2.36e-145 36 976 3 806
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
1.58e-147 36 1008 81 910
Lysosomal alpha-glucosidase OS=Mus musculus OX=10090 GN=Gaa PE=1 SV=2
6.56e-145 36 1008 81 910
Lysosomal alpha-glucosidase OS=Rattus norvegicus OX=10116 GN=Gaa PE=2 SV=1
9.29e-144 36 976 81 884
Lysosomal alpha-glucosidase OS=Homo sapiens OX=9606 GN=GAA PE=1 SV=4
1.40e-141 36 976 81 884
Lysosomal alpha-glucosidase OS=Pongo abelii OX=9601 GN=GAA PE=2 SV=1
1.86e-141 88 1008 55 894
Lysosomal alpha-glucosidase OS=Bos taurus OX=9913 GN=GAA PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000325 0.999647 CS pos: 18-19. Pr: 0.9852

TMHMM  Annotations      download full data without filtering help

Start End
1117 1139