CAZyme Information: MGYG000001537_02412

Basic Information

• Species: Cellulomonas timonensis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas timonensis
• CAZyme ID: MGYG000001537_02412
• CAZy Family: GH11
• CAZyme Description: Bifunctional xylanase/deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
657		67913.01	8.6213

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001537	4057828	Isolate	not provided	not provided

• Gene Location: Start: 762218; End: 764191 Strand: -

Full Sequence      

MSDRLVLDRAMPRRRRLARALLSIGAAAAMAASGLVAAGPATAAVTSNQTGNNGGYFYSF
WTDAPGTVSMELGASGNYSTQWSNTGNFVAGKGWSTGGRKTVNYSGSFNPSGNAYLTLYG
WSTNPLVEYYIVDNWGTYRPTGTFKGTVTSDGGTYDIYETTRTNQPSIEGTATFKQFWSV
RQSKRTGGTITTGNHFDAWASKGMNLGTHNYMIMATEGYQSSGNSNITVSEGSGGGNPTP
TPTSGGGGSSGCTVTATRGDEWSDRFNVSYAVSGSSSWTVNLGLNGSQSIQNSWNANVSG
SGSTRTVTPNGNGNTFGVTIMKNGNSSTPSATCAGGGGGGSTPTPTTQPTTTPTTPSTGG
WTGSCSAGYVGLTFDDGPTSGTSSQLINTLKQNGATATVFPTGQNAQNNASLMRAYADAG
LQIGNHSWDHPHLINMSSSEIQSQLSRTQTAIQQTSGVTPKLFRPPYGETNATLKQVESS
LGLREIIWDVDSQDYNNGSADQIRQAAQRLTNGQIILMHDWPANTIAALPNILQDLKSRN
LCPGVISADTGRAVAPGTSTGGGTGGGGSTGSCAVTATRGDEWSDRFNVTYSVSGSSAWT
VNLALNGSQSIQSSWNATVSGSGSTRTVKPNGNGNSFGVTVMKNGNSTTPGATCTTG

Enzyme Prediction     

EC	3.2.1.8	3.1.1.72

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH11	55	228	5.2e-78	0.9887005649717514
CE4	368	484	3.8e-27	0.8769230769230769
CBM2	252	337	9.9e-18	0.9702970297029703
CBM2	573	656	8.5e-17	0.9504950495049505

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00457	Glyco_hydro_11	1.73e-103	54	226	1	175	Glycosyl hydrolases family 11.
cd10953	CE4_SlAXE_like	1.03e-89	368	546	1	179	Catalytic NodB homology domain of Streptomyces lividans acetylxylan esterase and its bacterial homologs. This family is represented by Streptomyces lividans acetylxylan esterase (SlAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. SlAXE 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 result of deacetylation. SlAXE also functions as a chitin and chitooligosaccharide de-N-acetylase with equal efficiency to its activity on xylan. SlAXE forms a dimer. Each monomer contains a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases, which encompasses a mononuclear metalloenzyme employing 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. SlAXE possess a single metal center with a chemical preference for Co2+.
cd10917	CE4_NodB_like_6s_7s	3.65e-65	368	537	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	2.88e-50	369	539	2	170	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.
cd10954	CE4_CtAXE_like	1.60e-49	369	539	2	170	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEE44519.1	6.49e-311	1	657	1	645
VEH26523.1	6.49e-311	1	657	1	645
CAA54145.1	9.72e-308	1	657	1	644
QHT57826.1	1.14e-303	1	657	1	661
AEI13495.1	2.68e-286	51	657	30	626

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZSE_A	1.34e-108	44	229	1	186	3DStructure of a thermophilic family GH11 xylanase from Thermobifida fusca [Thermobifida fusca]
5EJ3_A	6.52e-104	12	229	7	230	Crystalstructure of XlnB2 [Streptomyces lividans],5EJ3_B Crystal structure of XlnB2 [Streptomyces lividans]
1M4W_A	1.01e-103	45	229	4	188	Thermophilicb-1,4-xylanase from Nonomuraea flexuosa [Thermopolyspora flexuosa]
7EO6_A	1.05e-102	45	229	6	190	ChainA, Endo-1,4-beta-xylanase [Actinomycetia bacterium],7EO6_B Chain B, Endo-1,4-beta-xylanase [Actinomycetia bacterium]
1HIX_A	6.94e-102	45	229	4	189	CrystallographicAnalyses Of Family 11 Endo-Beta-1,4- Xylanase Xyl1 From Streptomyces Sp. S38 [Streptomyces sp. S38],1HIX_B Crystallographic Analyses Of Family 11 Endo-Beta-1,4- Xylanase Xyl1 From Streptomyces Sp. S38 [Streptomyces sp. S38]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54865	1.94e-308	1	657	1	644	Bifunctional xylanase/deacetylase OS=Cellulomonas fimi OX=1708 GN=xynD PE=1 SV=1
D7EZJ3	2.92e-125	11	334	19	338	Endo-1,4-beta-xylanase B OS=Streptomyces sp. OX=1931 GN=xynBS9 PE=1 SV=1
P26515	9.17e-107	12	272	7	270	Endo-1,4-beta-xylanase B OS=Streptomyces lividans OX=1916 GN=xlnB PE=1 SV=3
Q59674	8.81e-105	45	556	30	586	Bifunctional xylanase/xylan deacetylase OS=Cellvibrio japonicus OX=155077 GN=xyn11A PE=1 SV=1
Q9RI72	1.45e-94	25	229	31	239	Endo-1,4-beta-xylanase C OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=xlnC PE=3 SV=1

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
0.000883	0.694920	0.000252	0.303268	0.000436	0.000215

TMHMM  Annotations     

start	end
21	43