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CAZyme Information: MGYG000002190_01197

You are here: Home > Sequence: MGYG000002190_01197

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 Clostridium sp001916075
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp001916075
CAZyme ID MGYG000002190_01197
CAZy Family GH16
CAZyme Description Beta-glucanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
241 MGYG000002190_9|CGC3 27362.49 5.6305
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002190 2598727 MAG Spain Europe
Gene Location Start: 68778;  End: 69503  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002190_01197.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 36 236 3e-92 0.9757281553398058

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02175 GH16_lichenase 3.54e-121 31 240 1 212
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 2.07e-57 31 238 47 264
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
pfam00722 Glyco_hydro_16 5.28e-53 59 236 1 167
Glycosyl hydrolases family 16.
cd00413 Glyco_hydrolase_16 8.80e-37 42 236 12 207
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.
cd02176 GH16_XET 9.49e-27 55 190 10 142
Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16. Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Xyloglucan is a soluble hemicellulose with a backbone of beta-1,4-linked glucose units, partially substituted with alpha-1,6-linked xylopyranose branches. It binds noncovalently to cellulose, cross-linking the adjacent cellulose microfibrils, giving it a key structural role as a matrix polymer. Therefore, XET plays an important role in all plant processes that require cell wall remodeling.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AGF58046.1 2.46e-136 1 241 6 246
AQR96736.1 2.86e-135 1 241 6 246
ADL52419.1 2.97e-135 1 241 1 247
BCZ45550.1 3.88e-133 1 240 6 245
BCZ47763.1 5.71e-133 11 241 16 246

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3I4I_A 8.14e-115 29 241 22 234
Crystalstructure of a prokaryotic beta-1,3-1,4-glucanase (lichenase) derived from a mouse hindgut metagenome [uncultured murine large bowel bacterium BAC 14],3I4I_B Crystal structure of a prokaryotic beta-1,3-1,4-glucanase (lichenase) derived from a mouse hindgut metagenome [uncultured murine large bowel bacterium BAC 14]
1MAC_A 3.93e-96 29 238 2 209
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]
3O5S_A 1.34e-95 20 238 19 235
CrystalStructure of the endo-beta-1,3-1,4 glucanase from Bacillus subtilis (strain 168) [Bacillus subtilis]
3WVJ_A 1.71e-94 36 240 13 215
ChainA, Beta-glucanase [Acetivibrio thermocellus ATCC 27405],3WVJ_B Chain B, Beta-glucanase [Acetivibrio thermocellus ATCC 27405]
1BYH_A 3.98e-94 27 238 2 211
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P45797 1.66e-98 23 238 22 235
Beta-glucanase OS=Paenibacillus polymyxa OX=1406 GN=gluB PE=3 SV=1
P23904 3.74e-97 23 238 21 234
Beta-glucanase OS=Paenibacillus macerans OX=44252 PE=1 SV=2
P04957 1.80e-96 8 238 11 239
Beta-glucanase OS=Bacillus subtilis (strain 168) OX=224308 GN=bglS PE=1 SV=2
P07980 3.78e-95 1 238 1 236
Beta-glucanase OS=Bacillus amyloliquefaciens OX=1390 GN=bglA PE=3 SV=1
A3DBX3 3.96e-92 36 240 42 244
Beta-glucanase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=licB PE=1 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
0.000218 0.999090 0.000183 0.000179 0.000159 0.000150

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002190_01197.