CAZyme Information: MGYG000001514_04050

Basic Information

• Species: Paenibacillus_A ihumii
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
• CAZyme ID: MGYG000001514_04050
• CAZy Family: GH11
• CAZyme Description: Bifunctional xylanase/deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
355	MGYG000001514_12|CGC47	38658.93	8.0481

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001514	5923787	Isolate	not provided	not provided

• Gene Location: Start: 2810634; End: 2811701 Strand: -

Full Sequence      

MKAKRMKLFAAFLLCFTLALPGAVHAQTITSNSVGTHDGYDYEYWKDSGNGTMVLGSGGT
FSAEWSNINNILFRKGKKFNETQTHQQIGNISITYGATYQPNGNSYLTVYGWTVDPLVEY
YIVDSWGSWRPPGASPKGTVNVDGGTYDIYETTRVNQPSIKGTATFKQYWSVRTSKRTSG
TISVSEHFKAWEKLGMTMGKMYEVALTVEGYQSSGSANVYSHTLTIGGGTTPPPTTGTKI
EAESMTKSGQYTGNISSPFNGVALYANNDSVKFTHNFTTGTHNFSLRGASNNSNMARVDL
KIGGQTKGTFYFGGSSPAVYTLNNVSHGTGNQEVELVVTADNGTWDAFIDYLEIH

Enzyme Prediction     

EC	3.2.1.8	3.1.1.72

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH11	38	219	2.4e-76	0.9887005649717514
CBM36	241	354	1.4e-53	0.991304347826087

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00457	Glyco_hydro_11	1.19e-88	38	218	1	175	Glycosyl hydrolases family 11.
cd04078	CBM36_xylanase-like	5.62e-64	239	354	3	118	Carbohydrate Binding Module family 36 (CBM36); appended mainly to glycoside hydrolase family 11 (GH11) domains; xylan binding. This family includes carbohydrate binding module family 36 (CBM36) most of which appear appended to glycoside hydrolase family 11 (GH11) domains. These CBMs are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH11 catalytic modules with their dedicated, insoluble substrates. GH11 domains have xylanase (endo-1,4-beta-xylanase) activity which catalyzes the hydrolysis of beta-1,4 bonds of xylan, the major component of hemicelluloses, to generate xylooligosaccharides and xylose. This family includes XynB from Dictyoglomus thermophilum Rt46B.1 and Xyn11A from Pseudobutyrivibrio xylanivorans Mz5T. Xyn11A is a multicatalytic enzyme with an N-terminal GH11 domain, a CBM36 domain, and a C-terminal putative NodB-like polysaccharide deacetylase which is predicted to be an acetyl esterase involved in debranching activity in the xylan backbone. 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. Consistent with its structural and sequence similarity to CBM6, CBM36 binds xylan, but only at binding site I, and in a calcium-dependent manner; the latter suggests its potential application in affinity labeling.
pfam03422	CBM_6	8.24e-07	241	354	1	123	Carbohydrate binding module (family 6).
cd02795	CBM6-CBM35-CBM36_like	3.04e-05	239	354	1	124	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZK47932.1	8.28e-250	1	355	1	354
AVI01407.1	5.77e-246	1	355	1	356
QXF28299.1	3.54e-213	4	354	16	376
ABB77852.1	3.38e-211	4	354	16	376
CAM82403.1	1.30e-210	4	354	5	365

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6KJL_A	1.34e-195	27	354	1	327	XylanaseJ from Bacillus sp. strain 41M-1 [Bacillus sp. 41M-1],6KJL_B Xylanase J from Bacillus sp. strain 41M-1 [Bacillus sp. 41M-1]
2DCJ_A	4.92e-195	29	354	29	353	Atwo-domain structure of alkaliphilic XynJ from Bacillus sp. 41M-1 [Bacillus sp. 41M-1],2DCJ_B A two-domain structure of alkaliphilic XynJ from Bacillus sp. 41M-1 [Bacillus sp. 41M-1],2DCK_A A tetragonal-lattice structure of alkaliphilic XynJ from Bacillus sp. 41M-1 [Bacillus sp. 41M-1]
6KKA_A	1.06e-194	29	354	2	326	XylanaseJ mutant from Bacillus sp. 41M-1 [Bacillus sp. 41M-1],6KKA_B Xylanase J mutant from Bacillus sp. 41M-1 [Bacillus sp. 41M-1]
7AYP_A	8.36e-171	26	354	1	352	Structureof a GH11 domain refined from the X-ray diffraction data of a GH11-CBM36-1 crystal. [uncultured bacterium]
2F6B_A	3.04e-125	29	228	3	203	Structuraland active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp. (NCL 87-6-10). [Bacillus],2F6B_B Structural and active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp. (NCL 87-6-10). [Bacillus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P83513	2.74e-166	26	351	15	362	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
Q8GJ44	9.40e-109	4	342	3	366	Endo-1,4-beta-xylanase A OS=Thermoclostridium stercorarium OX=1510 GN=xynA PE=1 SV=2
P33558	1.79e-105	4	342	3	367	Endo-1,4-beta-xylanase A OS=Thermoclostridium stercorarium OX=1510 GN=xynA PE=1 SV=2
P17137	3.97e-102	27	227	60	260	Endo-1,4-beta-xylanase OS=Clostridium saccharobutylicum OX=169679 GN=xynB PE=3 SV=1
P00694	7.36e-102	1	227	1	227	Endo-1,4-beta-xylanase A OS=Bacillus pumilus OX=1408 GN=xynA PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000238	0.999051	0.000184	0.000182	0.000164	0.000151

TMHMM  Annotations     

start	end
7	29