dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: VBB86764.1

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Basic Information help

Species

Podospora comata

Lineage

Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora comata

CAZyme ID

VBB86764.1

CAZy Family

GT32

CAZyme Description

Putative Glycoside Hydrolase Family 16

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
395	LR026970\|CGC9	44105.71	4.8960

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcomataTmat	13100	N/A	2652	10448

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in VBB86764.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH16	125	312	2e-90	0.9739583333333334

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185683	Glyco_hydrolase_16	5.91e-40	88	312	2	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.
185684	GH16_lichenase	5.42e-17	152	310	58	209	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.
395585	Glyco_hydro_16	4.43e-11	152	263	23	122	Glycosyl hydrolases family 16.
225182	BglS	1.69e-07	164	299	119	246	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
185692	GH16_fungal_CRH1_transglycosylase	5.77e-06	161	266	45	138	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
1.82e-297	1	395	1	395
2.49e-295	1	395	1	395
2.80e-141	41	367	55	392
1.03e-122	13	393	3	380
1.97e-111	37	375	15	336

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.73e-13	163	326	14	180	NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS [Paenibacillus macerans]
2.25e-12	163	384	14	227	Engineered Bacillus Bifunctional Enzyme Gluxyn-1 [Bacillus subtilis],1AXK_B Engineered Bacillus Bifunctional Enzyme Gluxyn-1 [Bacillus subtilis]
1.61e-11	163	317	14	157	NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS [Paenibacillus macerans]
2.11e-11	163	316	70	212	Crystal Structure 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]
2.18e-11	163	316	72	214	MOLECULAR AND 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
1.55e-10	163	316	95	237	Beta-glucanase OS=Paenibacillus macerans OX=44252 PE=1 SV=2
2.87e-10	163	316	96	238	Beta-glucanase OS=Paenibacillus polymyxa OX=1406 GN=gluB PE=3 SV=1
1.43e-08	155	295	88	219	Beta-glucanase OS=Bacillus amyloliquefaciens OX=1390 GN=bglA PE=3 SV=1
2.01e-08	155	295	92	223	Beta-glucanase OS=Bacillus licheniformis OX=1402 GN=bg1 PE=1 SV=1
2.68e-08	155	310	91	241	Beta-glucanase OS=Bacillus subtilis (strain 168) OX=224308 GN=bglS PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.300136	0.699863	CS pos: 43-44. Pr: 0.6637

TMHMM Annotations help

There is no transmembrane helices in VBB86764.1.