CAZyme Information: MGYG000003661_02266

Basic Information

• Species: Acetatifactor sp900554205
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900554205
• CAZyme ID: MGYG000003661_02266
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
363	MGYG000003661_156|CGC1	40896.05	4.2187

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003661	3177635	MAG	Peru	South America

• Gene Location: Start: 32467; End: 33558 Strand: -

Full Sequence      

MKLHDDYEDHSGMTPTVVMTIVAVTAFVAVILVVVLIMNSANKKPGQSAQETVSQETSPV
ILSPEPERYVSEGVLHPDDLDFWDKYPEEVEATPEPEQSLPQEEVKNDPSTDGKHTLVEK
SDGTEEWVLISPYLPKNEYDFTKLVCQSDFMKYYENGKQTSYVGVDVSKVQDYIDFVKVK
KAGIQFVMIRVGARGYGTGQLIVDDYFSENIKRATDAGLDVGVYFYSQAISKDEAVEEAN
LVLQQLGEYIISYPVAFDMELVTNDTARTDKLSKAERTEITKAFLDTIGAAGYKTIIYGN
KEWLIRQIDMSKLTAYDVWLSQQADIPDYPYKFTMWQYNTQGTVDGIAGLVNLNISFIDY
AEK

Enzyme Prediction     

No EC number prediction in MGYG000003661_02266.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	165	347	2.3e-42	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.69e-76	164	357	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	1.32e-32	164	355	2	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	1.56e-26	165	347	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	3.98e-24	164	354	5	187	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	7.42e-19	164	354	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM01196.1	1.98e-157	1	363	1	373
QCT06482.1	1.88e-66	132	360	89	319
QYX28904.1	2.27e-63	111	363	25	291
ABX43465.1	2.96e-63	128	362	389	623
QEK18217.1	1.70e-62	134	357	73	298

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JIP_A	1.07e-07	161	354	13	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	3.82e-09	164	355	69	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	6.90e-09	164	355	69	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	9.28e-09	164	355	69	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
1.000085	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
15	37