CAZyme Information: MGYG000002559_00899

Basic Information

• Species: Lachnospira sp900551945
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp900551945
• CAZyme ID: MGYG000002559_00899
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
326	MGYG000002559_24|CGC1	36763.53	4.8547

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002559	2652289	MAG	China	Asia

• Gene Location: Start: 484; End: 1464 Strand: +

Full Sequence      

MGNSKRKLNIAAVLCVIFAITTIAGIAASLIILKNRHFYSDERLASIKQSASKDTINKIE
NRLAQGETMVSILRDIDPDKMVYVSGGTYVFANINHSLKMNTFSNGTFAKDSNNQITYSE
NGKVVSHKVIDVSKYQTSIDFAKVKNAGVEYAMVRCGYRSYGSGILTEDTSFNNYAAEAL
KNNIKIGAYFFSQAINVEEAKEEAEYVLNMIKPYQISGPVAIDVEEIFDDTYRQMHLSAS
QLTDVIITFCDRIKEAGYTPMIYSNLSSFIGNIELDRLENYEKWLAYYSDEPYFPYEMSM
WQYTDSGSIDGITGNVDLNISFKEWN

Enzyme Prediction     

No EC number prediction in MGYG000002559_00899.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	130	312	5.2e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	4.57e-85	128	322	2	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	1.80e-37	128	320	1	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	1.13e-28	130	312	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	1.15e-27	128	319	1	182	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.
COG3757	Acm	1.00e-26	128	319	64	251	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR72973.1	2.98e-111	5	326	3	335
QNM03294.1	2.16e-70	41	325	91	380
AOZ96288.1	2.89e-69	8	325	26	362
QEK18217.1	3.46e-64	120	323	95	299
ADL34306.1	1.39e-63	40	325	72	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.91e-12	82	320	221	466	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	4.59e-12	82	320	221	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
5JIP_A	8.52e-08	106	319	3	220	Crystalstructure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens],5JIP_B Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens]
5A6S_A	4.17e-07	128	325	23	205	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	2.55e-13	128	324	10	198	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	3.02e-13	128	319	2	178	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P76421	2.42e-08	130	320	70	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	2.42e-08	130	320	70	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	2.42e-08	130	320	70	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX 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
0.727264	0.049384	0.002945	0.000657	0.000321	0.219446

TMHMM  Annotations     

start	end
10	32