CAZyme Information: MGYG000002287_02036

Basic Information

• Species: Agathobaculum sp003481705
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Butyricicoccaceae; Agathobaculum; Agathobaculum sp003481705
• CAZyme ID: MGYG000002287_02036
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
604		65885.07	4.605

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002287	2881212	Isolate	China	Asia

• Gene Location: Start: 42725; End: 44539 Strand: +

Full Sequence      

MAYGTANSYARPRRRRRKRKSHYGVLALVIVLLIALIVLAVKLVTTAVSTVLGRTETHEI
VYQVDNKLGYCDGKTFDLEAAPYRDQSGNLFAPLQSLCDALQIDLTWDESTKSGTAVWNK
QTAEIKASSTKVQMGEESRNMAAAPSVKDGVVFIPAKDFCAAFSWKTAETAEEQGDLLII
SQKDDELTEDAIKQITDDVTKVLGPSEKQITGDSILMRTDSDKALVAGETKTMASDGEKL
GEGVMEQNGTKYVPLKAAMTALGGTAEFDGKKTWTVKYNDTETTVTTNGKFKIDGNRVKG
DDFTVWLDEEKDRFYVSAPALAQIIGRNYTDLGDGAFAFTTLSLDGLDSQKTYLDSLRSS
LSDAVDGDIPEADVYIALTFDDGPTGKIENYPNGLTNYLLDGLKERGAKATFFECGYRIK
EYSACMPRQLEEGSEIANHTMNHPDSRLTGLSREEVDVQINSNSELIKEKTGSLPTLLRP
VGGGVNDTVKAVAKEAGLPIINWSVDTEDWKYRDAEHVKQVIVEQAGDGDVVLMHDLYPT
SVKGALAAIDELQARTDKTYAFVTVSQLAAIHGITLEPGVVYNGLSSKVAQEIKDGTYSP
AEFT

Enzyme Prediction     

No EC number prediction in MGYG000002287_02036.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	375	500	2e-21	0.8769230769230769

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10954	CE4_CtAXE_like	1.94e-67	375	568	2	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.
cd10917	CE4_NodB_like_6s_7s	2.56e-56	375	553	2	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	1.51e-47	375	565	2	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.
COG0726	CDA1	1.11e-41	345	578	36	266	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
TIGR02764	spore_ybaN_pdaB	1.75e-35	376	568	8	190	polysaccharide deacetylase family sporulation protein PdaB. This model describes the YbaN protein family, also called PdaB and SpoVIE, of Gram-positive bacteria. Although ybaN null mutants have only a mild sporulation defect, ybaN/ytrI double mutants show drastically reducted sporulation efficiencies. This synthetic defect suggests the role of this sigmaE-controlled gene in sporulation had been masked by functional redundancy. Members of this family are homologous to a characterized polysaccharide deacetylase; the exact function this protein family is unknown. [Cellular processes, Sporulation and germination]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQR04984.1	8.25e-41	369	582	53	251
ANU42137.1	8.25e-41	369	582	53	251
QIA31874.1	8.25e-41	369	582	53	251
QUO39027.1	5.29e-40	369	582	38	236
QBB67048.1	1.15e-38	376	583	63	255

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6H8L_A	5.54e-39	376	571	12	192	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]
6H8N_A	3.83e-38	376	571	12	192	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]
5LFZ_A	3.42e-32	376	583	27	216	T48deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
2CC0_A	1.05e-25	375	554	6	173	Family4 carbohydrate esterase from Streptomyces lividans in complex with acetate [Streptomyces lividans],2CC0_B Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate [Streptomyces lividans]
7FBW_A	1.88e-25	360	568	103	299	ChainA, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A3Q0NBH7	8.17e-36	376	582	268	456	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness) OX=1334565 GN=pgdA PE=1 SV=1
Q8Y9V5	8.17e-36	376	582	268	456	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) OX=169963 GN=pgdA PE=1 SV=1
A0A0H3GDH9	8.17e-36	376	582	268	456	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain 10403S) OX=393133 GN=pgdA PE=2 SV=1
O34798	8.30e-36	376	571	280	460	Peptidoglycan-N-acetylmuramic acid deacetylase PdaC OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaC PE=1 SV=1
Q81AF4	7.56e-26	368	568	16	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

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
0.999983	0.000049	0.000000	0.000000	0.000000	0.000001

TMHMM  Annotations     

start	end
21	43