CAZyme Information: MGYG000000187_00222

Basic Information

• Species: Lachnospira sp003537285
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp003537285
• CAZyme ID: MGYG000000187_00222
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
389	MGYG000000187_2|CGC1	44232.11	4.2719

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000187	2804290	Isolate	China	Asia

• Gene Location: Start: 101178; End: 102347 Strand: -

Full Sequence      

MKKIIRIYVAIIASVCLFILFPADIYAVVIDVSSYNGFIQWDNMKNYIEGTIIRIGYGSD
IQSQDDAAAIRNMDECERLGIPYGVYLYSYALDYYDAASETAHALRLLKGRSPELGVWFD
MEDADGYKARNGLDVYSEGELLSDFCEMFVNAMRVSGYKTGVYANYNYFTNVLDLDRLKS
IPEMNIWLAHWGIDSPSLDCTMWQFGAVEIEDEEYDGNIYYSDYSVKKDDNTGETIHSDD
STANNINVFYQTKLSSGRWLPVVKNNEDYAGIRGQNITGLAITTDTGHIKYRVHVNSGWL
GFIDSRNTNINDYYNGYAGNDTPVDAVEIYYYTPDDIITSSGYHYAFYKVSPVNNNYYSP
QKDNSTDNGMDGYAGIFGHFIDRIQINIR

Enzyme Prediction     

No EC number prediction in MGYG000000187_00222.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	30	205	6.8e-28	0.943502824858757

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	5.26e-46	29	205	3	172	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	9.58e-17	29	220	2	186	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	1.10e-09	30	205	1	171	Glycosyl hydrolases family 25.
cd06523	GH25_PlyB-like	1.30e-09	29	205	2	159	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) 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	2.92e-09	30	199	3	155	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
ACR72312.1	1.43e-272	1	389	1	389
CAB1238899.1	9.34e-69	30	389	4	358
CAB1239111.1	4.26e-63	30	389	6	358
QKN24730.1	5.59e-47	30	232	4	210
CBL26419.1	7.01e-47	29	385	5	352

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	7.88e-11	29	168	271	407	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	1.86e-10	29	168	271	407	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000410	0.998861	0.000240	0.000163	0.000152	0.000150

TMHMM  Annotations     

start	end
7	29