dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

CAG-485 sp900542185

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900542185

CAZyme ID

MGYG000003035_02050

CAZy Family

GH5

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
587	MGYG000003035_36\|CGC1	64089.61	4.6148

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003035	3548444	MAG	Netherlands	Europe

Gene Location

Start: 27824; End: 29587 Strand: +

Enzyme Prediction help

EC	3.2.1.151	3.2.1.73	3.2.1.4

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH5	258	550	5e-95	0.9891304347826086

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	3.44e-51	258	550	16	269	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	1.85e-20	245	550	54	360	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	5.47e-12	34	119	1	82	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	4.55e-11	135	213	10	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	5.63e-07	62	119	4	60	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
QCD42340.1	7.32e-109	3	587	13	593
SCD22090.1	7.44e-108	11	587	11	566
ADY35478.1	1.70e-106	5	567	7	559
ASB50110.1	5.85e-106	2	580	3	573
SCM57160.1	3.88e-104	11	587	11	566

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OYC_A	2.54e-77	210	580	14	393	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	1.94e-76	210	580	14	393	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]
6WQY_A	8.27e-75	232	567	21	367	ChainA, Cellulase [Phocaeicola salanitronis DSM 18170]
3ZMR_A	1.99e-64	127	579	10	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]
3NDY_A	1.05e-62	235	564	12	325	Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_A The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A7LXT7	2.06e-63	127	579	45	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
P28623	2.82e-62	228	564	27	356	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P28621	9.85e-61	234	564	41	358	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
O08342	7.20e-60	234	579	39	398	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P23660	1.53e-58	224	580	15	363	Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 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
0.000000	0.000011	1.000025	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003035_02050.

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