CAZyme Information: MGYG000001255_01914

Basic Information

• Species: Faecalibacterium prausnitzii_F
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium prausnitzii_F
• CAZyme ID: MGYG000001255_01914
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
389	MGYG000001255_29|CGC1	42400.34	4.4523

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001255	2423712	MAG	Austria	Europe

• Gene Location: Start: 6831; End: 8000 Strand: -

Full Sequence      

MKKTFWKKCTVRGTAAALALALTFSLGAPLALAAQPEEPETAAAAQTQEVQETDRPTLLP
ETPELAAEDPEAPPAQATEAEENSVNQHTPENSVVLTPEQISEALDAGALNEAEAQCLDF
GSENGFWTWLVNFLFGWLDKAEPVYSGWRTTGGKTYYYSSTTHEPVTGIQSIDDKLYYFD
ADGVLQKGKTFGVDVSKYQKNIDWEQIKKAGVSFVIVRIGYRGYGASGTLVLDPMFEEHF
TNVKNAGLKVGVYFFSQATTEEEAKEEAFACAYVLNGRKLDYPIFFDTEASGASGGSGRA
DGLGVADRTKCAVAFCEEVKANGYKPGVYASTLWYRNRVDLSSLTKYTIWNAHYGVASSP
IDCALWQGTCTARLPGYKGDLDVNISYIG

Enzyme Prediction     

No EC number prediction in MGYG000001255_01914.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	193	376	1.5e-42	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.56e-66	191	387	2	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.
cd06525	GH25_Lyc-like	1.49e-23	192	384	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.
cd00599	GH25_muramidase	3.68e-23	192	385	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	2.58e-22	193	376	1	179	Glycosyl hydrolases family 25.
COG3757	Acm	4.12e-20	192	384	65	251	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
CBL02062.1	7.98e-167	58	389	143	477
AXB29809.1	4.57e-166	58	389	143	477
AXA82288.1	5.53e-152	51	389	146	497
QIA44074.1	3.99e-147	33	389	122	498
ATP00196.1	4.43e-146	33	389	197	573

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.50e-15	192	384	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.49e-14	192	384	22	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]
1JFX_A	1.34e-12	192	384	7	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	4.05e-08	192	387	18	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
2X8R_A	2.37e-06	192	277	6	82	Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	1.91e-11	192	384	84	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	6.79e-10	192	384	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P33486	9.69e-08	189	375	3	188	Lysozyme OS=Lactococcus phage mv1 OX=33769 GN=lysA PE=1 SV=3

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
0.000717	0.998250	0.000431	0.000202	0.000190	0.000166

TMHMM  Annotations     

start	end
13	35