CAZyme Information: MGYG000004593_01572

Basic Information

• Species: CAG-194 sp000432915
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-194; CAG-194 sp000432915
• CAZyme ID: MGYG000004593_01572
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
536	MGYG000004593_21|CGC1	60101.72	4.4194

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004593	2619374	MAG	France	Europe

• Gene Location: Start: 45608; End: 47218 Strand: -

Full Sequence      

MSDSFYKQPNRFSSRQNKRKRRSQRIKMICVLLFALFAVSFLVFTIQKVRSDFRESGDIQ
TADAISSIAPAEIEIDGQEEEDTSLFTVCIDAGHGGKDIGSDSKGRIEKDDTLKLAKALS
DALSERQIRVVMTRDDDSFLYLSQRCKAATEANARYLISLHRNKGKGNGAEAWINSRASD
ETTSLASNILTSLEKVGISRNRGIKQGSYNSNEEDYYITANAEMPACILELGFINDSDDN
RMYDANLTDYANAIADAVMTTYECYKDQETCTNTIPDAKPDQNGLQLTNAVIENIEALDG
ECIGYGQGTNADEENRPVTSVQYEEQYKNYHAHFVNMDAPLTEDGAKKIYLTIDEGYEYG
TTASMLDTLQEKGVKATFFVTLPYAQSEPDLIRRMISEGHVIGNHSTTHPSAGLPSQDIE
TQKNEILQTDAYVREQYDYSMYLFRFPAGKFSEQSLAIVNNCNYESIFWSFAYLDYDVDN
QPDQAESLQKMISRLHPGAIYLLHGQSATNAAVLGDFIDQARELGYEFCLIEPDVQ

Enzyme Prediction     

No EC number prediction in MGYG000004593_01572.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	343	465	2e-23	0.9076923076923077

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10948	CE4_BsPdaA_like	1.22e-96	305	528	3	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.
TIGR02884	spore_pdaA	1.06e-69	310	528	6	217	delta-lactam-biosynthetic de-N-acetylase. Muramic delta-lactam is an unusual constituent of peptidoglycan, found only in bacterial spores in the peptidoglycan wall, or spore cortex. The proteins in this family are PdaA (yfjS), a member of a larger family of polysaccharide deacetylases, and are specificially involved in delta-lactam biosynthesis. PdaA acts immediately after CwlD, an N-acetylmuramoyl-L-alanine amidase and performs a de-N-acetylation. PdaA may also perform the following transpeptidation for lactam ring formation, as heterologous expression in E. coli of CwlD and PdaA together is sufficient for delta-lactam production. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
cd02696	MurNAc-LAA	1.93e-48	87	258	1	171	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.
cd10917	CE4_NodB_like_6s_7s	2.98e-44	347	522	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.
pfam01520	Amidase_3	6.70e-43	88	258	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VCV22796.1	8.68e-174	17	528	2	521
AEN96049.1	8.69e-163	88	528	70	550
BBF42562.1	6.58e-75	303	534	92	316
QNK40789.1	5.38e-68	292	528	63	290
CCO06017.1	2.62e-67	294	528	54	278

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2J13_A	9.10e-38	341	528	49	235	Structureof a family 4 carbohydrate esterase from Bacillus anthracis [Bacillus anthracis str. Ames]
1W1A_1	6.00e-37	296	532	16	244	Structureof Bacillus subtilis PdaA in complex with NAG, a family 4 Carbohydrate esterase. [Bacillus subtilis],1W1A_2 Structure of Bacillus subtilis PdaA in complex with NAG, a family 4 Carbohydrate esterase. [Bacillus subtilis],1W1B_1 Structure of Bacillus subtilis PdaA with Cadmium, a family 4 Carbohydrate esterase. [Bacillus subtilis],1W1B_2 Structure of Bacillus subtilis PdaA with Cadmium, a family 4 Carbohydrate esterase. [Bacillus subtilis]
1W17_A	7.00e-37	296	532	22	250	Structureof Bacillus subtilis PdaA, a family 4 Carbohydrate esterase. [Bacillus subtilis],1W17_B Structure of Bacillus subtilis PdaA, a family 4 Carbohydrate esterase. [Bacillus subtilis]
1NY1_A	2.61e-35	347	532	43	227	CrystalStructure Of B. Subtilis Polysaccharide Deacetylase Northeast Structural Genomics Consortium Target Sr127. [Bacillus subtilis],1NY1_B Crystal Structure Of B. Subtilis Polysaccharide Deacetylase Northeast Structural Genomics Consortium Target Sr127. [Bacillus subtilis]
4RN7_A	1.52e-19	83	269	1	185	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q04729	7.96e-37	341	528	61	247	Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1
O34928	3.83e-36	296	532	22	250	Peptidoglycan-N-acetylmuramic acid deacetylase PdaA OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaA PE=1 SV=1
P54525	1.39e-21	87	268	31	206	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
P02963	5.38e-20	342	504	18	174	Chitooligosaccharide deacetylase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=nodB PE=3 SV=3
P50355	8.23e-19	340	504	11	171	Chitooligosaccharide deacetylase OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=nodB PE=3 SV=2

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
0.999979	0.000050	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
28	47