CAZyme Information: MGYG000002528_00980

Basic Information

• Species: Anaerostipes hadrus
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerostipes; Anaerostipes hadrus
• CAZyme ID: MGYG000002528_00980
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
259		29752.24	9.6409

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002528	3172613	Isolate	China	Asia

• Gene Location: Start: 946418; End: 947197 Strand: -

Full Sequence      

MLDQDEKMKLTKKNKKELKMICGVLIFFAVIFIWIVQNIGLPIKTQVEKGRIKVIDISSY
NGTVNWKKVKDHNINHAMIKIGSGMNEKRAGRKDSKFDTNFRNAGYASIHRGVYYYSYAK
TTSDAKKEARHCLKLLKEQGIDPTDLDLPVAFDIEEEAVFQTGRRNVTAVTTTFCDEIKK
AGFEPMVYSGASALRNYFEYSKIREYKIWVAHYTKASAPAIPFSYDMWQYTSRAVINGAN
TGMGYCDLNYYLVDKNYKE

Enzyme Prediction     

No EC number prediction in MGYG000002528_00980.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	55	238	1.7e-46	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	2.59e-65	52	250	1	189	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	5.71e-34	53	251	1	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	7.45e-34	55	238	1	179	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	1.08e-28	53	251	1	184	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.
cd06524	GH25_YegX-like	3.43e-28	55	251	3	192	YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL39141.1	4.19e-185	6	259	2	255
AQP40897.1	1.53e-184	8	259	1	252
QCP33809.1	7.29e-112	9	255	3	249
BCD34460.1	4.87e-110	9	255	3	249
QMW72493.1	4.87e-110	9	255	3	249

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	4.89e-13	52	249	20	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.41e-12	52	249	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]
2WAG_A	2.83e-09	48	251	12	206	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	5.01e-07	48	240	1	194	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
3HMC_A	7.15e-07	54	255	7	183	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.83e-11	48	249	5	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	4.36e-06	48	240	78	271	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P34020	6.44e-06	52	238	1	170	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
P33486	8.02e-06	117	225	64	175	Lysozyme OS=Lactococcus phage mv1 OX=33769 GN=lysA PE=1 SV=3

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
1.000025	0.000008	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
21	43