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CAZyme Information: MGYG000000517_02173

You are here: Home > Sequence: MGYG000000517_02173

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 UMGS1889 sp900556055
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UMGS1889; UMGS1889 sp900556055
CAZyme ID MGYG000000517_02173
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
264 29664.95 4.292
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000517 2612851 MAG Fiji Oceania
Gene Location Start: 13352;  End: 14146  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 59 257 2.5e-87 0.9611650485436893

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02175 GH16_lichenase 1.76e-119 52 261 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.
pfam00722 Glyco_hydro_16 7.24e-53 79 247 1 163
Glycosyl hydrolases family 16.
COG2273 BglS 4.81e-51 66 261 62 267
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd00413 Glyco_hydrolase_16 7.80e-47 76 242 24 195
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 2.57e-27 75 210 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
QIB59261.1 1.14e-118 52 264 48 261
CBL06694.1 1.14e-118 52 264 48 261
BDA09400.1 3.26e-118 52 264 48 261
SNV04827.1 1.32e-117 53 264 49 261
BAL82171.1 7.58e-108 52 264 48 263

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WVJ_A 4.38e-91 60 261 17 215
ChainA, Beta-glucanase [Acetivibrio thermocellus ATCC 27405],3WVJ_B Chain B, Beta-glucanase [Acetivibrio thermocellus ATCC 27405]
3I4I_A 1.88e-88 60 261 33 233
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 6.08e-77 61 260 14 210
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]
1BYH_A 6.50e-77 60 260 15 212
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]
3O5S_A 1.00e-76 60 260 39 236
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
A3DBX3 9.91e-89 60 261 46 244
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
Q84C00 2.27e-87 60 261 46 244
Beta-glucanase OS=Acetivibrio thermocellus OX=1515 GN=licB PE=1 SV=1
O14412 1.13e-79 53 259 40 240
Beta-glucanase OS=Orpinomyces sp. (strain PC-2) OX=50059 GN=licA PE=1 SV=1
Q53317 3.19e-79 54 259 577 786
Xylanase/beta-glucanase OS=Ruminococcus flavefaciens OX=1265 GN=xynD PE=3 SV=2
P45797 3.37e-77 60 260 39 236
Beta-glucanase OS=Paenibacillus polymyxa OX=1406 GN=gluB PE=3 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
0.000003 0.000219 0.999804 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000517_02173.