CAZyme Information: MGYG000002215_01270

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia
• CAZyme ID: MGYG000002215_01270
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
361	MGYG000002215_40|CGC1	39777.92	6.4679

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002215	3457696	MAG	Spain	Europe

• Gene Location: Start: 400; End: 1485 Strand: +

Full Sequence      

MALNGIDVSQYQGDIDWNQVKNSGIEFAMIRGGFGKNNIDPYFHQNAKECQRLKLPMGIY
WFSYALSADMAAKEAQYCIALAKQYTITWPLAYDLEYDSLRYAAQNGVTITKQLATDMAR
AFCETIKAAGYIPMNYMNLDYYQTMFYMSQLPYDLWLAQYASAPSITHMEMWQYTSQGKV
PGISGNCDKNYSYKDYSSGSILPSPSPSAPEEYTVQPGDTLSEIALRFGTTVASLAAINN
ISDPNKIYAGQVLRLAGNPVQGETYVVKSGDTLSGIAAKYGTTYQSLAQANGISNPDFIY
PGQVIKIPGGSQSAARYYTILPGDTLSGIAQKFGTTVSRLQSLNQISNPDKIYAGNRIRI
S

Enzyme Prediction     

No EC number prediction in MGYG000002215_01270.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	183	1e-45	0.9943502824858758
CBM50	265	308	9.1e-18	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.74e-83	5	193	3	191	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599	GH25_muramidase	2.85e-33	5	191	2	185	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
pfam01183	Glyco_hydro_25	3.72e-29	6	183	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	1.85e-26	5	190	5	187	Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd06525	GH25_Lyc-like	1.42e-25	4	191	1	183	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEK16471.1	2.28e-107	1	360	1	325
QYX27151.1	1.03e-100	1	360	1	325
QHB23957.1	6.43e-77	1	255	1	265
QEI31463.1	6.43e-77	1	255	1	265
QRT30197.1	6.43e-77	1	255	1	265

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	5.48e-14	3	185	16	196	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
2WW5_A	1.52e-11	6	193	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	2.03e-11	6	193	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
3HMC_A	2.24e-11	6	190	8	177	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
5JCD_A	2.01e-10	213	308	85	192	Crystalstructure of OsCEBiP [Oryza sativa Japonica Group],5JCD_B Crystal structure of OsCEBiP [Oryza sativa Japonica Group],5JCD_C Crystal structure of OsCEBiP [Oryza sativa Japonica Group]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q49UX4	3.38e-30	213	361	29	194	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
Q2G0U9	9.52e-27	197	361	13	202	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=sle1 PE=1 SV=1
Q7A1T4	9.52e-27	197	361	13	202	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MW2) OX=196620 GN=sle1 PE=3 SV=1
Q5HIL2	9.52e-27	197	361	13	202	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain COL) OX=93062 GN=sle1 PE=3 SV=1
Q2FJH7	9.52e-27	197	361	13	202	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain USA300) OX=367830 GN=sle1 PE=3 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
1.000029	0.000013	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002215_01270.