CAZyme Information: MGYG000004256_00668

Basic Information

• Species: CAG-177 sp003538135
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; CAG-177; CAG-177 sp003538135
• CAZyme ID: MGYG000004256_00668
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
410		45478.75	9.6008

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004256	2314164	MAG	China	Asia

• Gene Location: Start: 44930; End: 46162 Strand: +

Full Sequence      

MDIKRRFAGAAAVLLACIAALLFAALVPARAISPSGGRRYRGIDISEFQGEVDFGKVRRS
GIEAVYIRAGAGEYADEYFAENYSQAREAGLRVGFYHYVTARSVEAGRRQARFFASLAAG
RRLDMRLAMDFEYFGSLTAEQVNAIAEAYLDELTRVTKKEAVIYSDLSNARSVFGRRLAE
KYPLWAAQYGADEPSSNGKWREWVGFQYTDKGRVDGISGDVDRDIFTEGIFLSSACRTDG
EKKSPKREKTRTVILYVRPGDTLWKIAREYGTTVKAVAEENRIANPDMIFAGERLKITLP
ARDGREEIYTVKRGDTPISIAGKYGVSLSALEHRNGLRRGETIYAGEKLIIPGAKMSGEF
YAVRPGDTLWSISRKTGVALEELIGINGIKDPDLIYAGEHIKLKGRKSCP

Enzyme Prediction     

No EC number prediction in MGYG000004256_00668.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	43	217	1.2e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	2.85e-66	41	226	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.
cd00599	GH25_muramidase	4.92e-53	41	226	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.
cd06414	GH25_LytC-like	3.46e-49	41	226	2	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.
pfam01183	Glyco_hydro_25	9.50e-46	43	217	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	4.90e-39	40	231	63	258	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
QJS18123.1	3.40e-108	27	408	20	401
QBE96304.1	5.93e-97	31	403	25	402
QWT55024.1	2.15e-96	27	405	23	410
QIB56830.1	9.45e-96	31	403	25	402
QMW80393.1	9.45e-96	31	403	25	402

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.55e-40	41	235	21	216	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	7.42e-39	41	235	21	216	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]
1JFX_A	1.91e-22	41	226	6	202	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	2.32e-17	34	228	16	203	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2WAG_A	1.55e-12	41	226	17	206	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
P26836	4.46e-38	41	231	10	201	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.42e-28	41	239	2	193	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
P25310	2.73e-22	30	226	72	279	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P76421	8.15e-21	42	245	69	272	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	2.09e-20	42	245	69	272	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.034368	0.963480	0.000966	0.000585	0.000305	0.000260

TMHMM  Annotations     

start	end
7	29