logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001523_03784

You are here: Home > Sequence: MGYG000001523_03784

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 Gracilibacillus massiliensis
Lineage Bacteria; Firmicutes; Bacilli; Bacillales_D; Amphibacillaceae; Gracilibacillus; Gracilibacillus massiliensis
CAZyme ID MGYG000001523_03784
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
367 40871.38 3.7402
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001523 4207224 Isolate not provided not provided
Gene Location Start: 1452122;  End: 1453225  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.73 3.2.1.6 3.2.1.8 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 29 233 9.9e-82 0.9902912621359223
CBM6 266 365 1.6e-20 0.7101449275362319

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02175 GH16_lichenase 9.61e-102 27 236 2 212
lichenase, member of glycosyl hydrolase family 16. Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure.
COG2273 BglS 6.47e-59 29 334 50 355
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
pfam00722 Glyco_hydro_16 4.17e-45 55 233 1 168
Glycosyl hydrolases family 16.
cd00413 Glyco_hydrolase_16 1.51e-38 32 235 7 210
glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.
cd02183 GH16_fungal_CRH1_transglycosylase 2.89e-23 91 218 41 180
glycosylphosphatidylinositol-glucanosyltransferase. Group of fungal GH16 members related to Saccharomyces cerevisiae Crh1p. Chr1p and Crh2p are transglycosylases that are required for the linkage of chitin to beta(1-3)glucose branches of beta(1-6)glucan, an important step in the assembly of new cell wall. Both have been shown to be glycosylphosphatidylinositol (GPI)-anchored. A third homologous protein, Crr1p, functions in the formation of the spore wall. They belongs to the family 16 of glycosyl hydrolases that includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADU30622.1 1.64e-224 2 367 10 379
BAB06950.1 1.19e-182 67 367 1 302
AIC93358.1 3.89e-121 30 238 34 243
AHZ55735.1 3.89e-121 30 238 34 243
AUG58471.1 2.66e-82 29 366 41 413

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1BYH_A 3.17e-85 21 237 1 214
MOLECULARAND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE [synthetic construct],1GLH_A Cation Binding To A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity And Effect On Protein Stability [Paenibacillus macerans],2AYH_A Crystal And Molecular Structure At 1.6 Angstroms Resolution Of The Hybrid Bacillus Endo-1,3-1,4-Beta-D-Glucan 4- Glucanohydrolase H(A16-M) [hybrid]
1U0A_A 2.56e-84 21 237 1 214
ChainA, Beta-glucanase [Paenibacillus macerans],1U0A_B Chain B, Beta-glucanase [Paenibacillus macerans],1U0A_C Chain C, Beta-glucanase [Paenibacillus macerans],1U0A_D Chain D, Beta-glucanase [Paenibacillus macerans]
1MAC_A 1.55e-82 38 237 16 212
CrystalStructure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans],1MAC_B Crystal Structure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans]
1GBG_A 1.73e-79 21 235 1 212
BacillusLicheniformis Beta-Glucanase [Bacillus licheniformis]
3O5S_A 5.40e-79 21 235 25 236
CrystalStructure of the endo-beta-1,3-1,4 glucanase from Bacillus subtilis (strain 168) [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P45797 1.77e-82 34 237 38 238
Beta-glucanase OS=Paenibacillus polymyxa OX=1406 GN=gluB PE=3 SV=1
P23904 1.95e-81 38 237 41 237
Beta-glucanase OS=Paenibacillus macerans OX=44252 PE=1 SV=2
P04957 4.20e-79 6 235 7 240
Beta-glucanase OS=Bacillus subtilis (strain 168) OX=224308 GN=bglS PE=1 SV=2
P27051 3.48e-78 20 235 29 241
Beta-glucanase OS=Bacillus licheniformis OX=1402 GN=bg1 PE=1 SV=1
P07980 1.22e-77 20 234 25 236
Beta-glucanase OS=Bacillus amyloliquefaciens OX=1390 GN=bglA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000263 0.998983 0.000178 0.000211 0.000177 0.000165

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001523_03784.