CAZyme Information: MGYG000004852_00502

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium
• CAZyme ID: MGYG000004852_00502
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
999	MGYG000004852_77|CGC1	108314.02	6.8906

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004852	2526742	MAG	China	Asia

• Gene Location: Start: 1888; End: 4887 Strand: -

Full Sequence      

MGRNKKLLLLICLLFILNVFNFDVQALSSKSSSQAIGNVNIVSSTDTSLETVEAWARSKN
ATETFVGLAKIYKKYAESRGGVNWVLAYVQAAKETGYGKFGGVLDESYHNPCGLKNPSGG
YDYDADAHKKFDNWEQGVLAHLDHLALYAAANGFPKTTYVDKWKDEELASDETYDPRHIG
WFGTTNGILGKARDVLSLTGSWASDPNYGIELFRMYCDATNSEYLPAKSNLESPSNSEVI
NNGKLRVKGWALHAFGIKEIKVLVDNSQVATINTGISRLDVNSTYPGYFNGTNSGFDETI
DISNLGSGNKTVEVIIVARNGETQSYKRNIVVKGENVSLPKINSLDAPTNNSVVTDGNLQ
IRGWALDEAGVKEVRVYIDNKDFGTITYGTTRTDVNKAYPGYSSGNNAGFDGKIDVSSLT
SGNKNVVVKITSNDGTSKDIERTITIQKLQSRSSLDEPTNNSIAGSTTLKVRGWALDSSG
IKEVRVYVDGKDLGTVTYGTKRTDVNKAYPGYSSGDNAGFEGFVDISSIGTGTKKLSVKI
TANDGTTQTIDRTINVQRLQSRSNLDEPNNKITAKSTLKVRGWALDSSGVKEVRVYVDGK
DLGTVTYGTKRTDVNKAYPGYSSGDNSGFEGIVDISSVAAGDKKLTVKITANDGTTQTID
RTIKVEKLLSRSSLDEPTSNTTVASGQLKVRGWALADSGIKEVRVYVDNIDLGTITYGTT
RTDVNKAYPGYSSGDNAGFEGIINLGGMTTGDKKLTVKITANDGTTQIVERDIVYRQAKL
VVVDPGHEIESIDPGAVATHNGIRYVEANLNLQIAIKLKAELEAKGIQVYMTRYDGIVID
NDSTESLKKRVKIANEMNADLFVSIHHNSFTSSSANGFEVYYSTGTPITTYISERMITED
GRDLTLEMSSYTSRSTTDKVSISKALATAITNEASSTLGLYNRGAKDSNLYVCKNTTMPS
ILIENGFLTNPTEAAKVSTTGHQQKLAEITAKRINEVLK

Enzyme Prediction     

No EC number prediction in MGYG000004852_00502.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	1.17e-59	781	992	2	169	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	1.50e-53	781	988	1	166	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	4.89e-49	775	998	39	228	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
smart00646	Ami_3	2.09e-26	851	994	1	113	Ami_3 domain.
PRK10319	PRK10319	8.52e-25	779	994	57	272	N-acetylmuramoyl-L-alanine amidase AmiA.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYE34895.1	5.24e-204	3	994	4	1329
QAS60290.1	2.18e-179	3	773	4	774
QLY79091.1	6.90e-128	230	773	47	580
CCO12189.2	1.15e-98	229	995	726	1470
AGK97878.1	2.23e-86	225	764	37	581

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JWQ_A	1.94e-19	779	998	2	176	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5EMI_A	6.91e-15	780	999	6	179	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4RN7_A	8.28e-15	778	988	3	172	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
4BIN_A	8.59e-14	780	988	175	383	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
7RAG_B	4.82e-12	779	987	17	198	ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q02114	7.14e-18	781	988	322	485	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
P33772	1.75e-15	779	994	57	272	N-acetylmuramoyl-L-alanine amidase AmiA OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiA PE=3 SV=1
P36548	1.05e-14	779	994	57	272	N-acetylmuramoyl-L-alanine amidase AmiA OS=Escherichia coli (strain K12) OX=83333 GN=amiA PE=1 SV=1
P54525	1.97e-14	777	988	28	194	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q06320	4.97e-14	781	987	4	164	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000359	0.998930	0.000223	0.000173	0.000165	0.000156

TMHMM  Annotations     

start	end
7	29