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CAZyme Information: KDQ23169.1

You are here: Home > Sequence: KDQ23169.1

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 Pleurotus ostreatus
Lineage Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
CAZyme ID KDQ23169.1
CAZy Family AA3
CAZyme Description glycoside hydrolase family 31 protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
911 KL198013|CGC11 101297.17 5.4233
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PostreatusPC15 12460 1137138 164 12296
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.20:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 253 787 7.7e-141 0.9976580796252927

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269888 GH31_MGAM_SI_GAA 0.0 273 693 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 4.38e-180 254 787 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.
224418 YicI 4.95e-118 8 829 35 710
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
269889 GH31_GANC_GANAB_alpha 9.97e-105 279 828 7 467
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 5.00e-92 279 693 7 336
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 2 911 59 887
2.38e-308 2 911 67 990
2.38e-308 2 911 67 990
3.32e-282 14 910 71 971
8.82e-282 14 910 71 969

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.94e-154 29 868 73 851
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]
8.73e-152 3 910 56 871
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]
1.72e-151 3 910 56 871
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-acetyl-cysteine [Homo sapiens]
9.95e-151 3 910 58 873
Crystal structure of human GAA [Homo sapiens],5KZX_A Crystal structure of human GAA [Homo sapiens]
3.66e-128 8 911 58 869
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.80e-239 2 907 65 1056
Alpha-glucosidase OS=Candida tsukubaensis OX=5483 PE=1 SV=1
1.57e-231 1 886 62 919
Glucoamylase 1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=GAM1 PE=1 SV=3
1.81e-230 1 895 61 949
Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=agl1 PE=1 SV=2
7.13e-225 2 899 78 975
Uncharacterized family 31 glucosidase C1039.11c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC1039.11c PE=3 SV=1
1.14e-222 1 890 72 935
Glucoamylase 1 OS=Schwanniomyces occidentalis OX=27300 GN=GAM1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000059 0.000002

TMHMM  Annotations      help

There is no transmembrane helices in KDQ23169.1.