CAZyme Information: MGYG000001045_00417

Basic Information

• Species: Enterocloster sp005845215
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster sp005845215
• CAZyme ID: MGYG000001045_00417
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
525		58258.65	6.2564

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001045	5511723	MAG	Denmark	Europe

• Gene Location: Start: 14984; End: 16561 Strand: -

Full Sequence      

MDRRGIRPLDYGGQMEAEERAVSGRRSVSVRQTERRKQARRRARRRAFFLAAAELAAGVC
MTMAVMAMVIPENRESGNGQFLPGVHTEKTAFYRILDETARLQTSIKGEGEALCSILYRG
NTEYAGPPVIAVDAGHGGEDEGASQEGVMEKDINLAIAKRLKTKLEDMGYTVMMVREDDT
YHSKEQRVEAAHKVRAGAYVSIHQNTWEDTDIRGIETWYSEAGGAGDETQGSASSGDGAR
ASAGDSRRLAALIHKEAVGSTGAEARELRGDAEFTVTSQTSIPSCLIETGFLSNARERQC
LTDPEYQEKLAGGIAKGIDLYFKPRIMYLTFDDGPSAENTSAVLDVLKARNIKATFFVVG
QNVRKHPDVARRIVAEGHTIGIHCNRHDYKALYESRDSYLADFEEAYRAVLEVTGVRPVL
YRFPGGSINGYNQKVYKEIIAEMDARGFIYFDWNASLDDALKKSQPQELVDNAKKTILGR
RQVVLLAHDMVHSTSLCLDGLIDQLPEYRMEPLTPDVVPVQFKEQ

Enzyme Prediction     

No EC number prediction in MGYG000001045_00417.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	323	439	7.8e-27	0.8692307692307693

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10944	CE4_SmPgdA_like	1.09e-68	325	512	1	189	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.
cd02696	MurNAc-LAA	9.28e-58	129	319	1	172	N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
pfam01520	Amidase_3	6.23e-53	130	318	1	172	N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
COG0860	AmiC	2.11e-52	121	325	36	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd10917	CE4_NodB_like_6s_7s	1.75e-46	325	505	1	170	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJU23357.1	5.66e-273	1	525	1	515
QRP42504.1	1.51e-270	1	525	1	505
QIB68221.1	2.34e-47	323	522	96	298
QAT41967.1	8.84e-47	305	522	76	298
ABX40925.1	1.10e-46	284	523	79	322

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JMU_A	4.92e-27	325	514	20	214	ChainA, Peptidoglycan N-acetylglucosamine deacetylase [[Eubacterium] rectale ATCC 33656]
1JWQ_A	5.48e-24	129	321	3	175	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5EMI_A	5.05e-23	125	323	2	179	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
5NC6_A	6.82e-23	325	507	1	181	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	6.98e-23	325	507	2	182	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54525	7.26e-25	130	322	32	204	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q02114	2.55e-22	130	323	322	496	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
Q81EJ6	1.59e-21	325	507	69	249	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
O07596	4.70e-21	325	520	85	280	Putative polysaccharide deacetylase YheN OS=Bacillus subtilis (strain 168) OX=224308 GN=yheN PE=3 SV=1
Q9K0V3	5.00e-20	128	327	190	413	N-acetylmuramoyl-L-alanine amidase AmiC OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=amiC 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
0.999870	0.000132	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
47	69