dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Hungatella sp005845265

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella sp005845265

CAZyme ID

MGYG000000150_02160

CAZy Family

CE4

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
496		54900.81	4.8806

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000150	7470188	Isolate	United Kingdom	Europe

Gene Location

Start: 78494; End: 79984 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000000150_02160.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE4	295	410	5.2e-29	0.8615384615384616

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10944	CE4_SmPgdA_like	6.02e-74	297	484	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	9.16e-69	120	291	2	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	7.19e-66	120	290	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	4.49e-61	117	297	42	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd10917	CE4_NodB_like_6s_7s	3.33e-49	297	476	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJU23357.1	3.77e-179	118	494	136	512
QRP42504.1	3.08e-178	106	494	113	502
QOT12681.1	7.96e-49	108	476	52	461
AWP28024.1	2.73e-47	109	476	50	459
AYB44783.1	7.88e-47	108	426	52	412

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4RN7_A	4.99e-32	120	297	6	185	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5EMI_A	3.19e-27	119	290	6	174	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
5JMU_A	2.64e-26	297	486	20	214	ChainA, Peptidoglycan N-acetylglucosamine deacetylase [[Eubacterium] rectale ATCC 33656]
1JWQ_A	2.26e-23	119	297	3	179	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5NC6_A	4.66e-21	297	462	1	164	Crystalstructure 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 download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q02114	1.71e-33	120	294	322	495	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
P54525	6.52e-33	120	294	32	204	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
P50864	2.48e-29	119	297	42	232	Germination-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlD PE=1 SV=1
Q06320	1.22e-23	120	297	4	178	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
P37134	2.98e-23	120	295	4	176	N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999801	0.000177	0.000001	0.000001	0.000000	0.000036

TMHMM Annotations download full data without filtering help

start	end
20	39

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