CAZyme Information: MGYG000001405_01021

Basic Information

• Species: Ferdinandcohnia timonensis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_L; Ferdinandcohnia; Ferdinandcohnia timonensis
• CAZyme ID: MGYG000001405_01021
• CAZy Family: CE4
• CAZyme Description: Bifunctional xylanase/deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
232	MGYG000001405_1|CGC6	26510.56	4.7815

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001405	4608762	Isolate	not provided	not provided

• Gene Location: Start: 1022140; End: 1022838 Strand: -

Full Sequence      

MKRKLMISAVVILIVFLLLGGTYKLMNTRSFQLLGGLTQQVDTDQKVVALTFDDGPTENI
NEILSLLDKYDVNATFFLIGQDIEKYPEEAKKIVDAGHQVGNHTYSHNRMIFKSPSFIKS
EIEKTDQLIREAGYKGEIDFRPPNGKKLMGLPFYLNKVNKDTITWNIEPDSYYPTPVEKI
RYVKESIQPGSIILIHPMYEDIDIVIEEIEGIIRVLEDEGYSFVTVNELQGM

Enzyme Prediction     

No EC number prediction in MGYG000001405_01021.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	42	145	7.8e-30	0.7923076923076923

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10956	CE4_BH1302_like	1.01e-102	42	231	1	194	Putative catalytic NodB homology domain of uncharacterized BH1302 protein from Bacillus halodurans and its bacterial homologs. This family is represented by a putative polysaccharide deacetylase BH1302 from Bacillus halodurans. Although its biological function is unknown, BH1302 shows high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Both BH1302 and SpPgdA belong to the carbohydrate esterase 4 (CE4) superfamily. This family also includes many uncharacterized bacterial polysaccharide deacetylases.
cd10917	CE4_NodB_like_6s_7s	5.67e-52	46	196	1	153	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.
cd10954	CE4_CtAXE_like	1.33e-45	46	229	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.
pfam01522	Polysacc_deac_1	9.29e-42	41	146	2	107	Polysaccharide deacetylase. This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyzes glucosidic bonds in xylan.
cd10959	CE4_NodB_like_3	1.81e-40	46	196	1	154	Catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases. This family includes many uncharacterized bacterial polysaccharide deacetylases. Although their biological function still remains unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYF84350.1	1.39e-118	1	232	1	232
AZV63003.1	2.80e-118	1	232	1	232
QNK48567.1	2.80e-118	1	232	1	232
AMM94398.1	3.97e-118	1	230	1	230
AEG59073.1	4.62e-117	1	230	1	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LFZ_A	1.03e-32	46	229	25	203	T48deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
7FBW_A	1.34e-30	46	229	117	299	ChainA, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
6H8L_A	3.53e-26	37	230	1	190	Structureof peptidoglycan deacetylase PdaC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],6H8L_B Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
6HM9_A	1.98e-25	44	229	83	266	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]
6H8N_A	2.69e-25	37	230	1	190	Structureof peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S [Bacillus subtilis subsp. subtilis str. 168],6H8N_B Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34798	1.04e-23	39	230	271	458	Peptidoglycan-N-acetylmuramic acid deacetylase PdaC OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaC PE=1 SV=1
Q81AF4	2.25e-23	35	229	11	208	Peptidoglycan-N-acetylglucosamine deacetylase BC_3618 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=BC_3618 PE=1 SV=1
Q81EK9	7.94e-22	48	226	83	264	Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=BC_1960 PE=1 SV=1
Q04729	2.51e-21	42	229	63	253	Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1
Q8DP63	7.49e-21	45	229	267	447	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.858730	0.089492	0.049282	0.000292	0.000185	0.002043

TMHMM  Annotations     

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