CAZyme Information: MGYG000001813_00254

Basic Information

• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella
• CAZyme ID: MGYG000001813_00254
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
386	MGYG000001813_37|CGC1	41848.19	9.9344

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001813	1209022	MAG	Denmark	Europe

• Gene Location: Start: 1286; End: 2446 Strand: +

Full Sequence      

MRQNGSNVNGRSNARPTARRDLGQLPSGQRRGRRKPGAMYLNHSRGFSDRSARIGNGRSP
RRSSRLPYALIAVGCAFVLFVAAVVGYINRSVDVVLNGEQTAVRVGSTLQTLIDDQELTD
TYSAGDLLAVDDSVLKRHGGEKLSVKVDGKRVKQGKWDSRELTGGEKITIKDGRNVYEKH
EVQATTIEPKLKVEGTGAIEYVQTWGVQGRSEVWVGEQSGKTQDRGEVVPATDCIVACAS
VAPKGNEKVVALTFDEGPSGATKQILQVLKEKGVTATFFLSGDSVEGNPATAKAIVDAGC
EVGSNSYSDDSLKGEDRETVRKQISKGTDAIKSATGVKTMLLRAPYAAFDEQNWIDAMDR
WSRGISIRVIGCSTVPTSRSRRCWIR

Enzyme Prediction     

No EC number prediction in MGYG000001813_00254.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	245	358	4.8e-25	0.8538461538461538

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10917	CE4_NodB_like_6s_7s	5.39e-35	248	371	1	120	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.
pfam01522	Polysacc_deac_1	5.42e-34	244	351	3	110	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.
cd10954	CE4_CtAXE_like	4.01e-29	248	356	1	112	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.
cd10956	CE4_BH1302_like	2.09e-26	246	347	3	105	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.
COG0726	CDA1	2.14e-25	246	351	63	169	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIA34238.1	5.17e-236	1	366	1	366
AZH70515.1	2.37e-211	39	366	1	328
ATP54936.1	3.37e-211	39	366	1	328
AEB06302.1	2.22e-110	33	359	34	354
QWT17787.1	4.02e-85	11	359	13	353

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7AX7_A	1.38e-18	245	348	1	105	Crystalstructure of the Xyl-CE4 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]
5LFZ_A	3.53e-16	230	348	17	125	T48deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
2C1G_A	2.91e-14	244	356	232	347	Structureof Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]
6H8L_A	1.04e-13	246	352	8	115	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]
2C1I_A	1.24e-13	244	356	232	347	Structureof Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant. [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P83513	2.94e-15	246	346	400	501	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
Q8DP63	1.76e-13	244	356	264	379	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1
P54865	7.40e-13	250	346	358	455	Bifunctional xylanase/deacetylase OS=Cellulomonas fimi OX=1708 GN=xynD PE=1 SV=1
Q5AQQ0	1.16e-12	229	351	27	143	Chitin deacetylase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cda PE=1 SV=1
O34798	4.27e-12	246	352	276	383	Peptidoglycan-N-acetylmuramic acid deacetylase PdaC OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaC 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
0.999906	0.000126	0.000005	0.000000	0.000000	0.000001

TMHMM  Annotations     

start	end
66	88