CAZyme Information: MGYG000000913_01291

Basic Information

• Species: Blautia sp900556555
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp900556555
• CAZyme ID: MGYG000000913_01291
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
339		38594.57	7.8703

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000913	2138636	MAG	China	Asia

• Gene Location: Start: 206; End: 1225 Strand: +

Full Sequence      

MPLNGIDVSQWQGEIDWKEVKNAGIKFAMIRAGYGKNNIDNKFHQNAQRAVQSGIPIGLY
WFSYAWNTEMATKEAQYTAALARQYKITWPIAYDLEYDTIEYARKNGVIITKNLATNMAK
AFCEEIERQGYIPMIYANLEYLNEYLDRSRLPYALWYAQYALEASVREKAIWQYTSEGSV
PGIQGAVDLDYGYKDYGSGNTVVPEETGPGGTVLELAAAVMEGKYGVGEERKKVLGNRYQ
EVQDFINHIARASTNTLVQEVWQGKYGNGEIRKVVLGGRYQEVQDKINDYQPYYYYTIRP
GDTLSGIAQRFGTTVKKLQSWNGIKNPDIIYAGTKIRVR

Enzyme Prediction     

No EC number prediction in MGYG000000913_01291.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	183	1.8e-46	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.11e-76	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	2.08e-40	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.
cd06413	GH25_muramidase_1	4.43e-34	2	189	2	186	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.
pfam01183	Glyco_hydro_25	4.45e-33	6	183	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	9.01e-29	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
QYX27151.1	7.11e-82	1	338	1	325
QEK16471.1	3.22e-80	1	338	1	325
AJE13220.1	1.29e-71	3	214	2	215
AXG90324.1	3.64e-71	3	214	2	215
ACQ51213.1	3.87e-71	3	214	4	217

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	2.01e-15	3	193	16	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	2.85e-14	3	190	20	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.04e-13	3	190	20	205	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	3.87e-13	3	188	5	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WW5_A	4.00e-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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	5.77e-15	3	190	9	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	5.47e-12	3	188	82	275	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
O34669	5.53e-07	296	339	80	122	Cell wall-binding protein YocH OS=Bacillus subtilis (strain 168) OX=224308 GN=yocH PE=1 SV=1
P37710	2.63e-06	295	339	498	541	Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2
Q99UM3	5.87e-06	296	338	177	219	Probable cell wall hydrolase LytN OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=lytN 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
1.000037	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000913_01291.