CAZyme Information: MGYG000001201_00201

Basic Information

• Species: CAG-451 sp900758495
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-451; CAG-451 sp900758495
• CAZyme ID: MGYG000001201_00201
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
470		53489.91	9.1143

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001201	1330564	MAG	Austria	Europe

• Gene Location: Start: 48994; End: 50406 Strand: +

Full Sequence      

MGKNMGINWWQQNKGKICLVFLIMLVFILLVFFLLVPRITLKGKSTIIVNRNGEYKEPGY
RASYLFDSLTDKVKVSGNVNSKKDGVYYITYKVKGPIITISTKRKVEVKDIEPPVITLEG
GADVFICPNSKYEELGYKANDNVDGDLTKRVEISRKDNIITYEVKDKAGNETKKMRKISE
GDKTPPVLTLNGGDIVFSYLGEPYVEPGYKAIDNCDQDITGMVITSGNVDKNNPNDQIIT
YTIEDKAHNKTEAKRTIKMVRRDHAGTIYLTFDDGPNAGTTNVILDILKEENVKATFFVT
GKGPDELIKREYDEGHTVALHTFSHSYPVVYQSVNAYFDDLEKVHDRVKRITGYDSRIIR
FPGGSSNTVSRHYQEGIMSILTNQVIEKGYYYYDWNISSGDAGEYRDSESIYKQVTRSLS
KDRTNMVLMHDIKPYTRDALRSIIKYGKEHGYHFDKITPGTKMVRQRVNN

Enzyme Prediction     

No EC number prediction in MGYG000001201_00201.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	264	370	1.3e-22	0.823076923076923

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10944	CE4_SmPgdA_like	2.30e-73	267	454	2	187	Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins. This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria.
cd10917	CE4_NodB_like_6s_7s	1.58e-44	266	446	1	169	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.
COG0726	CDA1	3.13e-32	246	454	44	250	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd10948	CE4_BsPdaA_like	1.39e-30	267	454	41	220	Catalytic NodB homology domain of Bacillus subtilis polysaccharide deacetylase PdaA, 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 pdaA gene encoding polysaccharide deacetylase BsPdaA, which is a member of the carbohydrate esterase 4 (CE4) superfamily. BsPdaA deacetylates peptidoglycan N-acetylmuramic acid (MurNAc) residues to facilitate the formation of muramic delta-lactam, which is required for recognition of germination lytic enzymes. BsPdaA deficiency leads to the absence of muramic delta-lactam residues in the spore cortex. Like other CE4 esterases, BsPdaA consists of a single catalytic NodB homology domain that appears to adopt a deformed (beta/alpha)8 barrel fold with a putative substrate binding groove harboring the majority of the conserved residues. It utilizes a general acid/base catalytic mechanism involving a tetrahedral transition intermediate, where a water molecule functions as the nucleophile tightly associated to the zinc cofactor.
cd10954	CE4_CtAXE_like	6.62e-30	268	454	3	174	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
QUO33814.1	6.75e-97	41	470	42	481
CBK81881.1	9.43e-96	73	470	74	477
ACR73576.1	1.63e-95	73	470	72	484
CBK91697.1	3.45e-89	42	470	38	489
CBK92741.1	4.87e-89	42	470	38	489

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JMU_A	5.74e-52	268	470	22	226	ChainA, Peptidoglycan N-acetylglucosamine deacetylase [[Eubacterium] rectale ATCC 33656]
5NC6_A	1.75e-22	269	455	4	187	Crystalstructure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide [Bacillus cereus]
5N1J_A	1.79e-22	269	455	5	188	Crystalstructure of the polysaccharide deacetylase Bc1974 from Bacillus cereus [Bacillus cereus],5N1J_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus [Bacillus cereus],5N1J_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus [Bacillus cereus],5N1J_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus [Bacillus cereus],5N1P_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with N-hydroxynaphthalene-1-carboxamide [Bacillus cereus],5N1P_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with N-hydroxynaphthalene-1-carboxamide [Bacillus cereus],5N1P_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with N-hydroxynaphthalene-1-carboxamide [Bacillus cereus],5N1P_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with N-hydroxynaphthalene-1-carboxamide [Bacillus cereus]
5NC9_A	4.37e-22	269	455	46	229	Crystalstructure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NC9_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NC9_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NC9_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NCD_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NCD_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NCD_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NCD_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NEK_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEK_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEK_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEK_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEL_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus],5NEL_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus],5NEL_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus],5NEL_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus]
5NC6_B	7.22e-22	269	455	72	255	Crystalstructure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide [Bacillus cereus],5NC6_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide [Bacillus cereus],5NC6_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide [Bacillus cereus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O07596	1.52e-25	267	454	86	270	Putative polysaccharide deacetylase YheN OS=Bacillus subtilis (strain 168) OX=224308 GN=yheN PE=3 SV=1
Q81EJ6	3.95e-21	269	455	72	255	Peptidoglycan-N-acetylglucosamine deacetylase BC_1974 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_1974 PE=1 SV=1
Q8DP63	1.28e-17	262	454	264	441	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1
Q04729	1.90e-17	268	457	69	250	Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1
Q8Y9V5	3.15e-16	268	454	268	439	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

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
1.000032	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
19	41