CAZyme Information: MGYG000002531_00042

Basic Information

• Species: Pseudobutyrivibrio fibrisolvens_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Pseudobutyrivibrio; Pseudobutyrivibrio fibrisolvens_A
• CAZyme ID: MGYG000002531_00042
• CAZy Family: GH11
• CAZyme Description: Bifunctional xylanase/deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
610	MGYG000002531_1|CGC1	66205.06	6.1759

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002531	3116879	Isolate	not provided	not provided

• Gene Location: Start: 43071; End: 44903 Strand: +

Full Sequence      

MKNKLTAALLAVVMTASLLVPSMTAKAADTIYNNKTGNQDGYDYELWKDTGNTSMTLNAG
GTFDCSWSNINNALFRKGKKFDSTKTYQQIGNITFDYGCDYRPNGNSYLCVYGWTVDPLV
EYYIVDSWGTWRPPGGSPKGQIQVDGGTYDVYETTRYNAPSIQGDTTFKQYFSVRTSKRT
SGTISVSEHFKAWERMGMRCGKLYEAALNIEGYQSSGSASVYKNNMTVGGSSSQGGNQGG
NQGGNTGNQGGSGNSGNTGTATGATVVQCENMTKSGQYTGNISSPFNGVALYANNDSVKY
TQYFASGTHDFTLRGCSNNNNMARVDLKIGGQTKGTFYYGDNYPAEYTIKNVSHGTGNQT
VELVVTADNGQWDAFLDYLSISGAGAAAGAGTGSSSNTGNNTGANTQNQKLIALTFDDGP
SSTTSQVLDVLERYGVKATFFLIGQNVNSNTMAIMQRQVRMGCELASHSYTHEDMSRMNP
SQIRNQMEWTSSAIKNTVGVDVKFFRPPYIAVNNSMYENIDVPFIQGSMHNDWEAGTSVS
QRVNSVLSSAKDGDIILLHDFQGNSQTVDALPQIIEGLKNQGYTFVTVSELFDKKGVNPD
VEYKIWSNVK

Enzyme Prediction     

EC	3.2.1.8	3.1.1.72

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH11	40	221	9.2e-75	0.9887005649717514
CBM36	269	380	2.6e-53	0.9739130434782609
CE4	405	513	1.5e-30	0.8153846153846154

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10954	CE4_CtAXE_like	1.22e-87	410	591	1	180	Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases.
pfam00457	Glyco_hydro_11	4.51e-82	40	220	1	175	Glycosyl hydrolases family 11.
cd04078	CBM36_xylanase-like	3.08e-64	264	379	1	116	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.
cd10917	CE4_NodB_like_6s_7s	3.96e-56	410	579	1	171	Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.
cd10944	CE4_SmPgdA_like	4.93e-49	410	585	1	187	Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins. This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAD65888.2	0.0	14	610	1	602
AMO13186.1	7.68e-311	2	608	3	783
ARI46381.1	2.01e-310	1	607	1	684
QJT73074.1	1.01e-199	14	382	1	348
AYV88967.1	5.73e-190	1	381	19	400

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7AYP_A	2.38e-204	28	385	1	356	Structureof a GH11 domain refined from the X-ray diffraction data of a GH11-CBM36-1 crystal. [uncultured bacterium]
2DCJ_A	2.46e-165	18	381	18	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	2.67e-165	31	381	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]
6KJL_A	3.92e-165	31	381	3	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]
7AYL_A	2.43e-131	2	230	3	231	Crystalstructure of the GH11 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium],7AYL_B Crystal structure of the GH11 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P83513	0.0	14	610	1	602	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
Q8GJ44	1.39e-104	3	229	6	232	Endo-1,4-beta-xylanase A OS=Thermoclostridium stercorarium OX=1510 GN=xynA PE=1 SV=2
P33558	4.24e-102	3	229	6	233	Endo-1,4-beta-xylanase A OS=Thermoclostridium stercorarium OX=1510 GN=xynA PE=1 SV=2
P17137	3.90e-99	24	229	55	260	Endo-1,4-beta-xylanase OS=Clostridium saccharobutylicum OX=169679 GN=xynB PE=3 SV=1
P00694	2.66e-92	28	229	27	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
0.000236	0.999040	0.000170	0.000199	0.000170	0.000152

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002531_00042.