dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Bacteroides congonensis

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides congonensis

CAZyme ID

MGYG000000675_00109

CAZy Family

GH128

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
443	MGYG000000675_1\|CGC5	49736.1	4.8511

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000675	5782172	MAG	Kazakhstan	Asia

Gene Location

Start: 150850; End: 152181 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000000675_00109.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH128	72	301	9.9e-57	0.9642857142857143
CBM6	347	442	2.7e-17	0.7318840579710145

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam11790	Glyco_hydro_cc	1.47e-56	71	302	14	235	Glycosyl hydrolase catalytic core. This family is probably a glycosyl hydrolase, and is conserved in fungi and some Proteobacteria. The pombe member is annotated as being from IPR013781.
cd04080	CBM6_cellulase-like	1.94e-18	319	442	4	144	Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase). This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities.
pfam18099	DUF5010_C	9.14e-10	336	439	2	110	DUF5010 C-terminal domain. This domain is found at the end of a family of putative glycosyl hydrolases pfam16402. This domain is likely to function as a carbohydrate binding domain due to its similarity with pfam03422.
cd04082	CBM35_pectate_lyase-like	1.32e-09	360	433	36	114	Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.
cd02795	CBM6-CBM35-CBM36_like	4.34e-08	319	437	1	118	Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIU93826.1	0.0	1	443	1	443
AIA99580.1	2.57e-85	1	439	1	439
QKX17146.1	2.19e-75	51	439	740	1114
QHQ40263.1	6.55e-74	51	439	741	1115
ACR13446.1	1.67e-67	49	440	722	1101

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6UAV_A	3.91e-53	51	305	2	256	Crystalstructure of a GH128 (subgroup II) endo-beta-1,3-glucanase from Pseudomonas viridiflava (PvGH128_II) [Pseudomonas viridiflava]
6UAW_A	7.56e-53	51	305	24	278	Crystalstructure of a GH128 (subgroup II) endo-beta-1,3-glucanase from Pseudomonas viridiflava (PvGH128_II) in complex with laminaritriose [Pseudomonas viridiflava]
6UAX_A	1.45e-36	47	304	88	344	Crystalstructure of a GH128 (subgroup II) endo-beta-1,3-glucanase from Sorangium cellulosum (ScGH128_II) [Sorangium cellulosum So ce56],6UAX_B Crystal structure of a GH128 (subgroup II) endo-beta-1,3-glucanase from Sorangium cellulosum (ScGH128_II) [Sorangium cellulosum So ce56]
6UAQ_A	1.81e-19	77	286	47	254	Crystalstructure of a GH128 (subgroup I) endo-beta-1,3-glucanase from Amycolatopsis mediterranei (AmGH128_I) [Amycolatopsis mediterranei],6UAR_A Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaritriose [Amycolatopsis mediterranei]
6UFL_A	4.56e-19	77	286	47	254	Crystalstructure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199Q mutant) from Amycolatopsis mediterranei (AmGH128_I) in the complex with laminarihexaose [Amycolatopsis mediterranei],6UFZ_A Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199Q mutant) from Amycolatopsis mediterranei (AmGH128_I) [Amycolatopsis mediterranei]