CAZyme Information: MGYG000000187_00121

Basic Information

• Species: Lachnospira sp003537285
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp003537285
• CAZyme ID: MGYG000000187_00121
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
507	MGYG000000187_1|CGC2	54762.24	4.2047

Genome Property

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

• Gene Location: Start: 121919; End: 123442 Strand: -

Full Sequence      

MSKLFKSDDDDFGYLDDSIHINWKKLLPAIIIIAVAVIALIIVLVVSFGHKGKKVPANAS
STEETSSVSETDTDGNNTLSDKDEKEQDPQYSDNDGAMNQDAGNGASVILSNSTNETSDV
TIGVDVSKFQGTIDWAQAASSGVDFAMIRVGYRAQKTGVIYADTNAKYNMQQAAANGIKV
GAYFFSSAVNEAEAIEEADWVADFIADYSITYPVAFDCEGFNTSESRQKSMTKAERTAVA
AAFLQEIYDKGYTPMFYAASSELTNNSQWNTASLESSYKIWVAQYPSTPYPETQSTSYAG
TCNMWQYTNQGRVAGIGTNVDINVAYFGYSESNSSLSGETAAAASPDVEAGMVFTSVNDT
VTAKDEVRLRDKPSQDTDAAVIATLVNGETITRTGTSSSGWSRLVYNGQTVYAVTSYLTT
DLTPKATESPTTGFNTKFTDCNDTVTPKEEVNLRNKPSVTDADSVVVATAKKGELFTRTG
YNTEVGWSRVVYNGQTLYCVTSLLSIQ

Enzyme Prediction     

No EC number prediction in MGYG000000187_00121.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	124	316	3.7e-45	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	7.60e-67	123	326	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	2.74e-32	123	325	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	2.23e-28	124	316	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	1.45e-22	123	326	5	190	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.
cd06523	GH25_PlyB-like	1.98e-22	124	323	3	175	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR73526.1	0.0	1	507	1	507
CBK93417.1	3.64e-173	80	507	51	484
CBK89713.1	5.16e-173	78	507	45	484
ACR77025.1	7.31e-173	78	507	45	484
CBK74296.1	2.98e-153	82	506	81	520

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	9.48e-09	116	323	1	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRT_A	5.02e-08	123	490	22	335	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]
4KRU_A	8.89e-08	123	323	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
3HMC_A	8.23e-07	124	317	8	172	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	2.00e-09	123	323	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.12e-07	116	323	78	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm 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
1.000046	0.000006	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
26	48