CAZyme Information: MGYG000002596_02026

Basic Information

• Species: Mediterraneibacter sp900555215
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900555215
• CAZyme ID: MGYG000002596_02026
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
307	MGYG000002596_78|CGC1	35421.86	3.7753

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002596	2662706	MAG	China	Asia

• Gene Location: Start: 7760; End: 8683 Strand: -

Full Sequence      

MDKRAGCITLVLFAAALCGCSDKENGAEKTIAEESVPQDQKESANEEAAEVEAQLEILDF
VDVFGQEYQVEINPNVEKHGYDLEKFVREGDRLTYTDDEYEYRLGVDVSRHQGWIDWERV
KASGYEFAIIRVGYRGYGEEGLVCLDEQFDTNIQNAQAAGLDVGVYFFAQAINEEEAKEE
AEFVLEHIAEYELQLPVVYDPESILDDEARTDDVSGEQFTKNTEVFCSMIEEAGYQPMIY
SNMLWEAYELDLEYLEEYPIWYADYEPFPQTPYHFDFWQYTNEGSVDGIEGRTDLNIQLI
PRKQIEE

Enzyme Prediction     

No EC number prediction in MGYG000002596_02026.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	106	289	5.6e-48	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.02e-73	105	297	3	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	1.19e-33	105	297	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.
cd06413	GH25_muramidase_1	4.38e-30	105	296	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.
pfam01183	Glyco_hydro_25	3.39e-26	106	289	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	1.52e-22	105	296	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
QRT51228.1	2.03e-117	3	302	2	287
QYX28904.1	9.59e-87	39	297	26	283
QRO38911.1	4.27e-85	39	297	26	283
QBF76167.1	4.27e-85	39	297	26	283
BBF45127.1	3.73e-81	48	300	24	278

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.93e-15	98	297	12	205	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	1.29e-06	105	170	7	66	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	3.24e-12	105	297	69	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	4.40e-12	105	297	69	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	8.13e-12	105	297	69	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P34020	8.70e-09	105	296	3	178	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	1.31e-07	105	296	11	194	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000001	1.000038	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002596_02026.