dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Prevotella salivae

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella salivae

CAZyme ID

MGYG000001360_00831

CAZy Family

GH5

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
576		63993.37	6.5793

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001360	3139873	Isolate	not provided	not provided

Gene Location

Start: 960279; End: 962009 Strand: -

Enzyme Prediction help

EC	3.2.1.4	3.2.1.-

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH5	256	540	1.3e-94	0.9855072463768116

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	8.05e-55	243	542	2	269	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	6.09e-19	224	565	46	386	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	1.88e-08	34	117	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	1.62e-05	127	209	5	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.
pfam13004	BACON	0.002	62	117	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
VEH16026.1	0.0	1	576	31	606
ADB44000.1	2.44e-121	130	576	49	513
SCD22090.1	5.09e-112	10	576	13	563
SCM57160.1	1.12e-110	10	576	13	563
ALJ60577.1	1.50e-105	21	573	25	595

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4W8A_A	7.87e-121	222	576	3	375	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]
5OYC_A	4.64e-69	217	574	40	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	3.50e-68	217	574	40	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]
6Q1I_A	9.87e-59	221	558	13	339	GH5-4broad specificity endoglucanase from Clostrdium longisporum [Clostridium longisporum],6Q1I_B GH5-4 broad specificity endoglucanase from Clostrdium longisporum [Clostridium longisporum]
6WQP_A	1.32e-57	221	565	15	348	GH5-4broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQP_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQV_A GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_C GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_D GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54937	3.40e-57	221	558	38	364	Endoglucanase A OS=Clostridium longisporum OX=1523 GN=celA PE=1 SV=1
P17901	1.92e-53	232	542	57	368	Endoglucanase A OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCA PE=1 SV=1
P23660	3.82e-53	221	539	26	327	Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 SV=1
P16216	1.09e-50	186	563	34	388	Endoglucanase 1 OS=Ruminococcus albus OX=1264 GN=Eg I PE=1 SV=1
P23661	6.03e-50	195	565	45	392	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
0.000025	0.014798	0.985180	0.000007	0.000009	0.000007

TMHMM Annotations help

There is no transmembrane helices in MGYG000001360_00831.

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