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CAZyme Information: MGYG000001664_01521

You are here: Home > Sequence: MGYG000001664_01521

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 CAG-485 sp900760735
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900760735
CAZyme ID MGYG000001664_01521
CAZy Family GH27
CAZyme Description Isomalto-dextranase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
469 MGYG000001664_31|CGC1 53319.25 4.783
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001664 3152185 MAG United States North America
Gene Location Start: 32813;  End: 34222  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001664_01521.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 194 447 9.4e-35 0.9388646288209607

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17801 Melibiase_C 5.54e-19 396 467 3 74
Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
PLN02229 PLN02229 9.60e-11 294 468 230 418
alpha-galactosidase
PLN02808 PLN02808 1.22e-10 294 468 200 384
alpha-galactosidase
cd14792 GH27 2.50e-09 68 381 14 271
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
cd14791 GH36 1.77e-06 118 239 67 178
glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNT67171.1 1.64e-227 3 467 6 473
QUU07210.1 6.12e-196 36 469 50 492
QUT44530.1 2.48e-195 36 469 50 492
QUT79686.1 2.48e-195 36 469 50 492
QRM98947.1 2.48e-195 36 469 50 492

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AWO_A 1.35e-98 44 468 37 466
Arthrobacterglobiformis T6 isomalto-dextranse [Arthrobacter globiformis],5AWP_A Arthrobacter globiformis T6 isomalto-dextranase complexed with isomaltose [Arthrobacter globiformis],5AWQ_A Arthrobacter globiformis T6 isomalto-dextranse complexed with panose [Arthrobacter globiformis]
1UAS_A 4.38e-15 177 468 97 360
ChainA, alpha-galactosidase [Oryza sativa]
4NX0_A 9.47e-15 79 468 49 441
Crystalstructure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q44052 1.49e-98 44 468 63 492
Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1
Q9FXT4 3.39e-14 177 468 152 415
Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000002 0.000029 1.000021 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001664_01521.