CAZyme Information: MGYG000000187_01806

Basic Information

• Species: Lachnospira sp003537285
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp003537285
• CAZyme ID: MGYG000000187_01806
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
662		71851.71	4.3448

Genome Property

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

• Gene Location: Start: 4515; End: 6503 Strand: +

Full Sequence      

MFSLKKLLKKDTISEQEAASQDSEYEVLEVTELSFIQTAKMWLRDFFRVKKHVIITAVSS
GAVVVAVAGIVITVSVVSRIGKQKSTDVAAAIEDTSTQMETAEEMKAPVLSLYLEAVADE
NTITASVYGEDGEILSGHELVFNLLSGSKEDNEEQIEKLKAAYAGQNVEDVDKEVYEDDD
KDGTVLMPDLETGTYTLVVQAEEGYKTPEAAEATVETFAVMDDIMEKVVADSAATQKEDP
SKNRSNSSPAVSVPETTASAGEVNVTALKKSGDNIIYKITGRSTMQLTDDEAARYTAGSV
LIDDHSVSAYSGYIYETGKIQITGGQADVVTKFLVPERNISTENVEMTNNTTVFADNLKE
TAAGTKETQSETKTTGESTKSEETSKTEETSKGENTKPSDNQSTTARKNYVLLSLEAETE
TVYADGWQNIQGKTYYFRNSQAVTGWNQIDGLQYYFNGDGSLGSHLVIDVSTYNGDIDWN
RVKAAGIDYAIIRVGYRGYETARLVKDKRFDTNMRNAIAAGVKVGAYIVTQAVNTNEAVE
EASFIISACSGYNVSLPLAIDVESAGNGKGRGDKISVAERTAVINAFVQTIRGAGYSAMV
YANKDWMTNRINAGGLVSGSTVWLAQYRSSCTYGGSYQMWQFTESGSIPGISGNVDMSAW
KY

Enzyme Prediction     

No EC number prediction in MGYG000000187_01806.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	468	651	5.8e-46	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	9.30e-78	467	660	3	190	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	2.00e-38	467	660	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	1.73e-35	468	651	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	1.01e-25	468	659	6	188	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	1.05e-25	468	657	3	181	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
ACR71183.1	0.0	1	662	1	662
AOZ95561.1	8.66e-58	278	658	823	1210
QNM02116.1	1.86e-56	402	658	824	1096
ADL33290.1	4.28e-56	416	658	980	1222
AVM48757.1	8.16e-55	457	660	12	213

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	2.16e-12	468	656	8	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	3.83e-10	463	658	18	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2WAG_A	9.06e-07	468	653	19	196	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	3.46e-11	468	656	85	275	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P34020	1.13e-09	468	657	4	177	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
P26836	3.90e-07	468	661	12	197	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc 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
0.999649	0.000335	0.000002	0.000001	0.000001	0.000004

TMHMM  Annotations     

start	end
54	76