CAZyme Information: MGYG000001525_03715

Basic Information

• Species: Paenibacillus_A rubinfantis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A rubinfantis
• CAZyme ID: MGYG000001525_03715
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
348		38561.29	9.0696

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001525	5369528	Isolate	not provided	not provided

• Gene Location: Start: 208074; End: 209120 Strand: -

Full Sequence      

MGRNKFAVIAICIAFVMILGQFAGIRAFVAKSSEQESGSFAFRLINDLTGDLGAQGKQDQ
KNGGAAKDMDPLLTYIRAESEKRRVEPIDAVVDRVWKAIPGYNGREVDIERTYVKAKQLP
EGAEIEYVYRELRPKVNLEDLGAQPIYRGNPNKPMAALMINVAWGNEYLVPMLDTLDKAK
VKATFFLDGSWLKKNVEMAAEIKRRGHQIENHAYSHPNMSQLEVTRARLEISKTKDLLKE
KLGVENRWFAPPSGDYNMQTVKLAAEQGLKTVLWTVDTVDWKNPPASSIVSKIGSKVGPG
SLILMHPTPSSRDALEGMIQAIQANGLQLGTVEQTLSPDRVDSPVPQS

Enzyme Prediction     

No EC number prediction in MGYG000001525_03715.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	148	272	2.1e-25	0.9384615384615385

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02873	spore_ylxY	3.09e-115	70	337	1	268	probable sporulation protein, polysaccharide deacetylase family. Members of this protein family are most closely related to TIGR02764, a subset of polysaccharide deacetylase family proteins found in a species if and only if the species forms endospores like those of Bacillus subtilis or Clostridium tetani. This family is likewise restricted to spore-formers, but is not universal among them in having sequences with full-length matches to the model. [Energy metabolism, Biosynthesis and degradation of polysaccharides, Cellular processes, Sporulation and germination]
cd10950	CE4_BsYlxY_like	1.85e-90	149	336	1	188	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.
TIGR02764	spore_ybaN_pdaB	2.47e-57	149	336	1	191	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]
cd10917	CE4_NodB_like_6s_7s	1.10e-52	154	323	1	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.
cd10949	CE4_BsPdaB_like	8.31e-49	152	337	2	191	Putative catalytic NodB homology domain of Bacillus subtilis putative polysaccharide deacetylase PdaB, 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 the putative polysaccharide deacetylase PdaB encoded by the pdaB gene on sporulation of Bacillus subtilis. Although its biochemical properties remain to be determined, the PdaB (YbaN) protein is essential for maintaining spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. The glycans of the spore cortex may be candidate PdaB substrates. Based on sequence similarity, the family members are classified as carbohydrate esterase 4 (CE4) superfamily members. However, the classical His-His-Asp zinc-binding motif of CE4 esterases is missing in this family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZS16060.1	3.19e-168	1	344	1	326
AZK47744.1	1.06e-149	1	344	1	326
AJS59120.1	9.15e-132	1	341	1	323
ANS74046.1	1.48e-131	3	344	5	341
AWP30845.1	7.71e-131	66	341	49	325

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7BKF_A	5.82e-82	69	342	1	274	ChainA, Putative polysaccharide deacetylase [Bacillus anthracis]
6HPA_A	1.99e-80	69	341	1	273	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme [Bacillus anthracis]
6HM9_A	2.12e-78	70	341	1	272	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]
4M1B_A	6.65e-34	142	337	45	244	StructuralDetermination of BA0150, a Polysaccharide Deacetylase from Bacillus anthracis [Bacillus anthracis],4M1B_B Structural Determination of BA0150, a Polysaccharide Deacetylase from Bacillus anthracis [Bacillus anthracis]
5O6Y_A	2.86e-30	147	332	14	204	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
P50850	3.72e-89	57	341	35	317	Uncharacterized protein YlxY OS=Bacillus subtilis (strain 168) OX=224308 GN=ylxY PE=3 SV=2
P50865	7.83e-30	127	332	30	239	Probable polysaccharide deacetylase PdaB OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaB PE=3 SV=2
Q81EK9	6.57e-29	147	332	74	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	1.01e-24	147	344	60	262	Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1
Q8DP63	1.44e-23	172	337	286	449	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
0.866909	0.094901	0.005260	0.000576	0.000337	0.032032

TMHMM  Annotations     

start	end
7	29