dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001643_01260

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Basic Information help

Species

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485;

CAZyme ID

MGYG000001643_01260

CAZy Family

GH5

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
583	MGYG000001643_30\|CGC1	63630.44	4.5574

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001643	4013444	MAG	United States	North America

Gene Location

Start: 1716; End: 3467 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.4

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH5	249	551	6.3e-96	0.9891304347826086

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	9.32e-49	249	549	16	267	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	2.12e-16	236	507	54	323	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	3.00e-14	130	214	3	83	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
cd14948	BACON	9.29e-12	33	119	1	83	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam13004	BACON	1.17e-06	154	214	2	61	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SCM57160.1	1.09e-160	6	581	11	566
SCD22090.1	6.36e-157	6	581	11	566
QUT37093.1	7.94e-151	6	581	13	593
QUT65987.1	5.07e-149	6	581	13	593
QUU01445.1	5.07e-149	6	581	13	593

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OYC_A	6.87e-115	225	576	44	395	GH5endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYC_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107]
6HA9_A	5.46e-114	225	576	44	395	Structureof an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HA9_B Structure of an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_A Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_B Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107]
4W8A_A	2.24e-90	224	581	1	378	Crystalstructure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in the native form [uncultured bacterium],4W8B_A Crystal structure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in complex with XXLG [uncultured bacterium]
3ZMR_A	2.38e-66	138	573	19	465	Bacteroidesovatus GH5 xyloglucanase in complex with a XXXG heptasaccharide [Bacteroides ovatus],3ZMR_B Bacteroides ovatus GH5 xyloglucanase in complex with a XXXG heptasaccharide [Bacteroides ovatus]
2JEP_A	7.08e-63	226	573	35	393	Nativefamily 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEP_B Native family 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEQ_A Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand [Paenibacillus pabuli]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A7LXT7	2.49e-65	138	573	54	500	Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02653 PE=1 SV=1
O08342	3.17e-62	225	573	39	398	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P28623	8.44e-49	226	573	43	371	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P28621	1.11e-43	225	576	41	376	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
P23661	5.65e-43	225	508	70	336	Endoglucanase B OS=Ruminococcus albus OX=1264 GN=celB 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
0.000004	0.003811	0.996237	0.000001	0.000002	0.000002

TMHMM Annotations help

There is no transmembrane helices in MGYG000001643_01260.