CAZyme Information: MGYG000003396_02402

Basic Information

• Species: Clostridium sp900766315
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900766315
• CAZyme ID: MGYG000003396_02402
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
889	MGYG000003396_123|CGC4	96898.61	8.0578

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003396	3926186	MAG	United States	North America

• Gene Location: Start: 36971; End: 39640 Strand: +

Full Sequence      

MKKNKSFLLLVCLIFMLNSFTFNVYALNSGTSSRAIGNVNIISTVDTSLERVEAWARSKN
ATETFVGLAKLYKKYAELRGGVNWVVAYVQAAKETGYGKFGGVLDESYHNPCGLKNPEDG
DDYDAGAHKKFDNWEQGVLAHLDHLALYAAADGFPKTSYLKNWKDEPLAENETYDPRHVG
WFGTTGGILGKAKDVLGLTGSWASDPNYGIELFRLYCDATNSEYLPAKSNLESPSNSEVI
TNGKLRIKGWALHAFGIKEIKVLVDKSQVATISTGLSRPDVNSTYPGYFNGDVSGFDQTI
DISGLGTGDKTVEVIIVARNGETQSYKRNIVIKEQNVNLPKLNNLEEPSNNKIITNGKLT
IKGWALDQSGVKEVRVSVDGKDFGNVNYGTTRTDVNKVYPGYPSGNNAGFEGTIDISNLT
SGNKKVVVQITSNDGSIQKIERTIKVEKLESKSWLDNPNNNSISSGTLRVSGWALASSGV
KEVRVYVDGKDLGTVNYGTTRTDVNNAYPGYPSGNNAGFEGSVNLSNISAGTKRVIVKIT
ANDGTSQSIERTIKVERLESKSWLDNPNNNSISSGTLRVSGWALASSGVKEVRVYVDGKD
LGTVNYGTTRTDVNNAYPGYPSGNNAGFEGTVNLGGMATGDKKLKVKITANDGTTQTIER
NFVYRKAKLVVVDPGHEIESVDPGASATHNGIRYVEGNLNLQIAVKLKAQLEAMGIEVYM
TRYDGLIIDKDSTESLKKRVKVANEMDADLFVSIHHNSYTSPSANGFEVYYSTGTPVSDN
MIARSLITEDGRDLTLERKSYRTRNIEEKVKVSKELATVITNTASTELGLYNRGAKDSNL
YVCKNTLMPSILIENGFITNPTEATKVSKDSHQQKLAEITAQKINEALK

Enzyme Prediction     

No EC number prediction in MGYG000003396_02402.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	4.56e-54	670	885	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	1.49e-47	670	878	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	4.07e-44	664	888	39	228	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
smart00646	Ami_3	3.89e-23	740	878	1	107	Ami_3 domain.
PRK10319	PRK10319	1.38e-21	668	884	57	272	N-acetylmuramoyl-L-alanine amidase AmiA.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYE34895.1	5.38e-162	41	884	41	1329
QAS60290.1	4.08e-159	41	660	41	658
QLY79091.1	2.99e-96	208	672	27	481
CCO12189.2	3.17e-77	225	878	831	1462
AGK97878.1	4.98e-68	225	655	37	466

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JWQ_A	3.18e-17	668	888	2	176	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A	1.15e-15	667	878	3	172	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5EMI_A	2.41e-15	669	884	6	174	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
7RAG_B	3.48e-11	668	877	17	198	ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile]
4BIN_A	3.81e-11	669	878	175	383	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q02114	1.05e-17	668	878	320	485	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
Q4L6X7	5.12e-15	666	878	118	279	Probable cell wall amidase LytH OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=lytH PE=3 SV=2
Q9K0V3	7.96e-15	669	881	191	401	N-acetylmuramoyl-L-alanine amidase AmiC OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=amiC PE=1 SV=1
P54525	1.72e-14	666	878	28	194	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
O48471	5.56e-14	667	888	2	181	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 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
0.000309	0.998918	0.000227	0.000182	0.000172	0.000160

TMHMM  Annotations     

start	end
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