CAZyme Information: MGYG000003124_01178

Basic Information

• Species: Rothia mucilaginosa_A
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Rothia; Rothia mucilaginosa_A
• CAZyme ID: MGYG000003124_01178
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
355		38191.44	4.963

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003124	1814262	MAG	United States	North America

• Gene Location: Start: 16075; End: 17142 Strand: +

Full Sequence      

MLPLIAACSNKSNNDYDSTSGNFTPYQAGSDSPSATPRPIATNSPTQSVTGNPIDKPREW
PGVGNALVGEGKYIAWTVDDGASPEAIRGYAEFSKRTNTRLTFFINASYVGFKNNVDILR
PLVQSGQIQIANHTYNHPDLTTLDAEGVKEELQRNEDEIMSIFGVSSKPYFRPPYGRYNE
AVLKAAGEIGFTRPVMWNGTTGDEAKTSARVIYMRSLRYMLPQQIVLGHLNYETIIPILD
KLKGLLDERGLTPVTIRDYYGDASEEEIKAAAPSPTATPEPSETPSAEATTEAPSPTPTP
TPTPAPTPRYEDEVAATRTPSQPAATTRASQPPQPAASRSTTASATAGAPAAANR

Enzyme Prediction     

No EC number prediction in MGYG000003124_01178.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	71	192	1.2e-23	0.8846153846153846

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10917	CE4_NodB_like_6s_7s	1.64e-44	72	242	1	166	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.
cd10950	CE4_BsYlxY_like	6.41e-31	70	258	4	186	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.
cd10951	CE4_ClCDA_like	8.89e-29	74	256	10	197	Catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41) from Colletotrichum lindemuthianum (also known as Glomerella lindemuthiana), which is a member of the carbohydrate esterase 4 (CE4) superfamily. ClCDA catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. It consists of a single catalytic domain similar to the deformed (alpha/beta)8 barrel fold adopted by 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. It possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Unlike its bacterial homologs, ClCDA contains two intramolecular disulfide bonds that may add stability to this secreted protein. The family also includes many uncharacterized deacetylases and hypothetical proteins mainly from eukaryotes, which show high sequence similarity to ClCDA.
cd10954	CE4_CtAXE_like	6.88e-28	72	255	1	176	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	5.16e-27	69	192	4	122	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCG43929.1	1.14e-23	71	229	41	196
ASF38113.1	1.14e-23	71	229	41	196
QNR20137.1	2.88e-23	72	229	42	198
ANU19959.1	4.45e-23	72	229	42	196
ASI34481.1	6.23e-23	72	229	42	198

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6HM9_A	6.37e-16	72	250	85	257	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]
6HPA_A	5.98e-14	72	250	86	258	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme [Bacillus anthracis]
7BKF_A	3.02e-13	72	250	86	258	ChainA, Putative polysaccharide deacetylase [Bacillus anthracis]
5LFZ_A	3.52e-13	72	270	25	214	T48deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
5O6Y_A	4.15e-13	74	265	23	213	Crystalstructure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q04729	1.37e-14	72	258	67	252	Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1
P04339	3.66e-13	70	229	19	174	Chitooligosaccharide deacetylase OS=Rhizobium leguminosarum bv. viciae OX=387 GN=nodB PE=3 SV=1
P50850	5.19e-13	74	229	132	282	Uncharacterized protein YlxY OS=Bacillus subtilis (strain 168) OX=224308 GN=ylxY PE=3 SV=2
P02963	1.75e-12	70	229	19	174	Chitooligosaccharide deacetylase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=nodB PE=3 SV=3
O34928	3.32e-12	72	258	66	251	Peptidoglycan-N-acetylmuramic acid deacetylase PdaA OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.042100	0.004442	0.953486	0.000003	0.000004	0.000003

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003124_01178.