CAZyme Information: MGYG000002881_00567

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus
• CAZyme ID: MGYG000002881_00567
• CAZy Family: GH11
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
937		100618.16	4.1151

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002881	1270591	MAG	United States	North America

• Gene Location: Start: 2149; End: 4962 Strand: +

Full Sequence      

MKNGFLRKLAAGVLSGLMCLVSVPTGIAANAADQQQTGNKDGYDYELWNQWGQGTATMDV
GSNGAFTCSWTGIENCLFRTGQKLGSTKSYTDYNGMYVDYDVDYEPKGNSYMCIYGWTED
PTVEYYIVEAWGSWRPPGSNDTLGTVTANGHTYDIYRTIRENQPSIHGTETFYQYWSVRR
DNPAQNNARKHIEGRISISKHFDAWQNAGLDMKGRMYEVALNIEGYQSAGSASVNKNGLV
IGKGDGDDGSSPDTPRPTVEPDSKGNYFYATFESGTDDWVGRGDAVTALNSKNYYAGSKS
LAVTGRTDNWHGAAISLDSDAFVPGQTYSFSTAVLQESGETTSMKLTLQYLLDGEDNYDE
VASADVKSGEWTKLENTAFTIPSGASNLVLYVEAPDSLTDFYIDEARGAVEGMKSDVVTG
GGTVDSGSVTPPTTTPSAAVVTTQAPTTVENPGSDNISWGDANCDGGVDIADATLILQVI
GNNDKYHLSEQGAKNADVFEAGSGITAMDALSVQKYDAGAIKSLPESYSEDWNGGNTTVT
DSPAQNPSDGKYFSNSFDSSTEGWTGRGDASIALNSDNYYSGKSLSVSGRTDNWNGAAVE
LDTKTFVPGIAYSFSAAVLQNSGAAETIQMTLQYTLDGEDNYEQIAVVTAKSGEWTKLEN
TSFTIPEGASDLLLYIEMPDSLADFYVDEVQTAEEGKKSSVVTGGGTVSDVPSTPPVEVG
SVDISWIDPSKPMVAISFDDGASPATGTRIVDALSDNGFHATFFYVGDWIRDTNGENEVK
YAYSKGMEIANHTKSHPNLTEKSASEIRSEYDQCASKLKGIIGAEPSNLLRLPYLGCNST
VQSTLSDVPLITCAIDTQDWNGASKEQIVNTIKSAISNGSLDGAIVLAHETYDTTASAME
ELCPYLKAQGWQIVTVSEMFAVKNQQLNGGQVYTKVN

Enzyme Prediction     

EC	3.2.1.8	3.1.1.72

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH11	41	234	1.4e-62	0.9887005649717514
CBM22	270	395	4.7e-34	0.9541984732824428
CBM22	554	679	3.2e-32	0.9618320610687023
CE4	729	845	4.9e-22	0.8538461538461538

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10954	CE4_CtAXE_like	1.33e-64	732	919	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	6.88e-64	41	233	1	175	Glycosyl hydrolases family 11.
cd10917	CE4_NodB_like_6s_7s	5.33e-45	732	907	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.
cd10947	CE4_SpPgdA_BsYjeA_like	6.99e-36	734	916	3	177	Catalytic NodB homology domain of Streptococcus pneumoniae peptidoglycan deacetylase PgdA, Bacillus subtilis BsYjeA protein, and their bacterial homologs. This family is represented by Streptococcus pneumoniae peptidoglycan GlcNAc deacetylase (SpPgdA), a member of the carbohydrate esterase 4 (CE4) superfamily. SpPgdA protects gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan N-acetylglucosamine (GlcNAc) residues. It consists of three separate domains: N-terminal, middle and C-terminal (catalytic) domains. The catalytic NodB homology domain is similar to the deformed (beta/alpha)8 barrel fold adopted by other CE4 esterases, which harbors a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The enzyme is able to accept GlcNAc3 as a substrate, with the N-acetyl of the middle sugar being removed by the enzyme. This family also includes Bacillus subtilis BsYjeA protein encoded by the yjeA gene, which is one of the six polysaccharide deacetylase gene homologs (pdaA, pdaB/ybaN, yheN, yjeA, yxkH and ylxY) in the Bacillus subtilis genome. Although homology comparison shows that the BsYjeA protein contains a polysaccharide deacetylase domain, and was predicted to be a membrane-bound xylanase or a membrane-bound chitooligosaccharide deacetylase, more recent research indicates BsYjeA might be a novel non-specific secretory endonuclease which creates random nicks progressively on the two strands of dsDNA, resulting in highly distinguishable intermediates/products very different in chemical and physical compositions over time. In addition, BsYjeA shares several enzymatic properties with the well-understood DNase I endonuclease. Both enzymes are active on ssDNA and dsDNA, both generate random nicks, and both require Mg2+ or Mn2+ for hydrolytic activity.
cd10950	CE4_BsYlxY_like	2.72e-31	728	920	2	188	Putative catalytic NodB homology domain of uncharacterized protein YlxY from Bacillus subtilis and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis putative polysaccharide deacetylase BsYlxY, encoded by the ylxY gene, which is a member of the carbohydrate esterase 4 (CE4) superfamily. Although its biological function still remains unknown, BsYlxY shows high sequence homology to the catalytic domain of Bacillus subtilis pdaB gene encoding a putative polysaccharide deacetylase (BsPdaB), which is essential for the maintenance of spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. However, disruption of the ylxY gene in B. subtilis did not cause any sporulation defect. Moreover, the Asp residue in the classical His-His-Asp zinc-binding motif of CE4 esterases is mutated to a Val residue in this family. Other catalytically relevant residues of CE4 esterases are also not conserved, which suggest that members of this family may be inactive.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL18305.1	1.22e-289	1	937	1	883
AEE64769.1	5.59e-201	1	937	1	757
AEE64770.1	4.81e-174	37	936	66	681
AAA85198.1	9.61e-170	1	937	1	680
ADU20638.1	1.91e-169	1	937	1	680

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7AYL_A	7.37e-71	1	242	1	230	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]
2F6B_A	2.61e-70	37	241	8	201	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]
1H4G_A	2.55e-68	38	241	9	201	Oligosaccharide-bindingto family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1H4G_B Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1QH6_A CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE [Salipaludibacillus agaradhaerens],1QH6_B CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE [Salipaludibacillus agaradhaerens],1QH7_A CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE [Salipaludibacillus agaradhaerens],1QH7_B CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE [Salipaludibacillus agaradhaerens]
1H4H_A	1.90e-67	38	241	9	201	Oligosaccharide-bindingto family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1H4H_B Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1H4H_C Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1H4H_D Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens]
2NQY_A	3.30e-67	37	241	8	201	Crystalstructure of alkaline thermophlic xylanase from Bacillus sp. (NCL 86-6-10) with complex xylotriose: Xylotriose cleaved to xylobiose and xylose [Bacillus sp. (in: Bacteria)],2NQY_B Crystal structure of alkaline thermophlic xylanase from Bacillus sp. (NCL 86-6-10) with complex xylotriose: Xylotriose cleaved to xylobiose and xylose [Bacillus sp. (in: Bacteria)]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q53317	2.78e-150	1	530	1	517	Xylanase/beta-glucanase OS=Ruminococcus flavefaciens OX=1265 GN=xynD PE=3 SV=2
P29126	8.48e-77	1	249	1	247	Bifunctional endo-1,4-beta-xylanase XylA OS=Ruminococcus flavefaciens OX=1265 GN=xynA PE=3 SV=1
P17137	3.01e-67	13	243	43	261	Endo-1,4-beta-xylanase OS=Clostridium saccharobutylicum OX=169679 GN=xynB PE=3 SV=1
Q8GJ44	8.13e-66	7	312	6	276	Endo-1,4-beta-xylanase A OS=Thermoclostridium stercorarium OX=1510 GN=xynA PE=1 SV=2
P83513	7.17e-65	20	411	6	368	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A 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
0.000327	0.998952	0.000163	0.000225	0.000175	0.000154

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002881_00567.