CAZyme Information: MGYG000003004_00081

Basic Information

• Species: Anaeromassilibacillus sp001305115
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Anaeromassilibacillus; Anaeromassilibacillus sp001305115
• CAZyme ID: MGYG000003004_00081
• CAZy Family: CBM50
• CAZyme Description: N-acetylmuramoyl-L-alanine amidase sle1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
108		12324.2	9.6969

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003004	2769057	MAG	United States	North America

• Gene Location: Start: 82556; End: 82882 Strand: -

Full Sequence      

MPAIVVYTVREGDTLWNIAKNFGTTVNDIARYNGLVDTDVLYPGQKLRIFVPDTNTNTSV
PKWYVVRPGDTLSRIAEKYGTTVQRLMWLNDIAVPDLIYPGQRLRIRP

Enzyme Prediction     

No EC number prediction in MGYG000003004_00081.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM50	64	106	1.3e-17	0.95
CBM50	7	49	1e-16	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK06347	PRK06347	1.22e-23	6	106	407	523	1,4-beta-N-acetylmuramoylhydrolase.
PRK06347	PRK06347	8.89e-23	6	106	332	449	1,4-beta-N-acetylmuramoylhydrolase.
PRK06347	PRK06347	1.65e-20	6	107	481	592	1,4-beta-N-acetylmuramoylhydrolase.
cd00118	LysM	3.87e-18	5	49	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
cd00118	LysM	1.79e-17	62	106	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUG56102.1	1.96e-25	1	106	32	138
ALP93086.1	1.32e-24	7	107	236	330
QBX22842.1	2.07e-24	7	106	219	315
ANU77129.1	4.19e-24	3	106	244	347
QJU17248.1	4.19e-24	3	106	244	347

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZ2_A	3.31e-08	7	49	5	46	Crystalstructure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_D Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ3_A Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8]
1E0G_A	8.29e-08	5	51	3	47	LYSMDomain from E.coli MLTD [Escherichia coli]
4XCM_A	1.84e-07	7	49	5	46	Crystalstructure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4XCM_B Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8]
5C8O_A	3.30e-06	8	49	62	103	Crystalstructure of MoCVNH3 variant (Mo0v) [Pyricularia oryzae],5C8P_A Crystal structure of MoCVNH3 variant (Mo0v) in complex with (N-GlcNAc)3 [Pyricularia oryzae],5C8Q_B Crystal structure of MoCVNH3 variant (Mo0v) in complex with (N-GlcNAc)4 [Pyricularia oryzae]
2L9Y_A	3.81e-06	8	49	66	107	Solutionstructure of the MoCVNH-LysM module from the rice blast fungus Magnaporthe oryzae protein (MGG_03307) [Pyricularia oryzae 70-15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q6GJK9	4.19e-19	7	106	93	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=sle1 PE=3 SV=1
P0C1U7	1.12e-18	7	106	93	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus OX=1280 GN=sle1 PE=3 SV=1
Q7A7E0	1.12e-18	7	106	93	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain N315) OX=158879 GN=sle1 PE=1 SV=1
Q5HIL2	1.12e-18	7	106	93	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain COL) OX=93062 GN=sle1 PE=3 SV=1
Q2G0U9	1.12e-18	7	106	93	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=sle1 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
1.000074	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003004_00081.