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CAZyme Information: PPTG_01216-t26_1-p1

You are here: Home > Sequence: PPTG_01216-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 parasitica
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
CAZyme ID PPTG_01216-t26_1-p1
CAZy Family AA17
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1142 123943.18 6.9093
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PparasiticaINRA-310 23240 761204 119 23121
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1:4 3.2.1.98:1 3.2.1.20:35 3.2.1.177:14

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 526 1017 1.7e-151 0.9929742388758782

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269888 GH31_MGAM_SI_GAA 0.0 544 927 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).
395838 Glyco_hydro_31 0.0 526 1017 2 442
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
224418 YicI 5.80e-142 344 1079 65 733
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
269889 GH31_GANC_GANAB_alpha 4.10e-135 544 1057 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 1.12e-119 544 930 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
1.02e-262 335 1141 61 891
7.11e-241 335 1109 55 853
7.97e-234 307 1102 37 821
3.26e-233 335 1103 58 850
1.14e-232 335 1103 63 854

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.58e-224 300 1100 37 851
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]
3.55e-173 328 1107 73 836
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]
3.55e-173 328 1107 73 836
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-acetyl-cysteine [Homo sapiens]
5.28e-173 328 1107 75 838
Crystal structure of human GAA [Homo sapiens],5KZX_A Crystal structure of human GAA [Homo sapiens]
4.74e-170 302 1141 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
2.17e-225 305 1100 37 847
Alpha-glucosidase OS=Spinacia oleracea OX=3562 PE=1 SV=1
6.99e-224 335 1100 61 849
Alpha-xylosidase 1 OS=Arabidopsis thaliana OX=3702 GN=XYL1 PE=1 SV=1
5.97e-223 336 1102 65 827
Probable alpha-glucosidase Os06g0675700 OS=Oryza sativa subsp. japonica OX=39947 GN=Os06g0675700 PE=1 SV=1
1.44e-221 338 1099 59 817
Alpha-glucosidase OS=Hordeum vulgare OX=4513 PE=2 SV=1
9.55e-217 300 1100 37 851
Alpha-glucosidase OS=Beta vulgaris OX=161934 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000016 0.000019

TMHMM  Annotations      help

There is no transmembrane helices in PPTG_01216-t26_1-p1.