CAZyme Information: MGYG000004417_00557

Basic Information

• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; UBA3631
• CAZyme ID: MGYG000004417_00557
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
350	MGYG000004417_3|CGC1	38313.85	9.4601

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004417	1346084	MAG	Israel	Asia

• Gene Location: Start: 64196; End: 65248 Strand: +

Full Sequence      

MDKVFGIDISTYQGGINLATAKAEGVKFALLRAGFTGYGNGVSKSVDNQFENHYRNAKAN
GLGVGAYWFSRATTYENGKAEAEYMYNNCLKGKQFEYPIAIDVEDSYYQAKAGKQAVTNA
IKGFCEYLEAKGYYVCIYANSNWFKNYMDLSQLTKYDKWVANWGTSRPSSPAGGLWQFGG
ETNRIRTNKVAGMTVDQNYAFYDYPAIMKQKGLNGFSANADVKPQDPVTPTPQPTPAPSN
DTIYVVKAGDTLSGIASKYGTTYQTLAAYNNISNPNLIYVGQQIKIPGNGTTTTNTTTNN
SKTYTVKSGDTLSGIASKYGTTWQKIYNDNKSVIGSNPNLIKPGQVLTIK

Enzyme Prediction     

No EC number prediction in MGYG000004417_00557.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	7	179	6.3e-39	0.9491525423728814
CBM50	244	287	4.1e-17	0.975
CBM50	304	349	5.9e-17	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.00e-59	5	201	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.
cd00599	GH25_muramidase	6.05e-32	6	181	2	171	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	5.14e-26	7	178	1	171	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	5.48e-26	6	171	2	155	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.
COG3757	Acm	1.41e-18	6	178	65	235	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
QEK16471.1	5.24e-64	4	349	3	325
QYX27151.1	9.11e-62	4	349	3	325
QHB22110.1	3.67e-51	1	217	1	215
QEI32774.1	3.67e-51	1	217	1	215
AZP03752.1	1.82e-50	3	214	2	208

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	3.56e-10	4	192	5	204	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	3.41e-08	3	199	15	200	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
5JCD_A	9.37e-07	243	349	84	191	Crystalstructure of OsCEBiP [Oryza sativa Japonica Group],5JCD_B Crystal structure of OsCEBiP [Oryza sativa Japonica Group],5JCD_C Crystal structure of OsCEBiP [Oryza sativa Japonica Group]
5JCE_A	2.08e-06	243	349	84	191	Crystalstructure of OsCEBiP complex [Oryza sativa Japonica Group],5JCE_B Crystal structure of OsCEBiP complex [Oryza sativa Japonica Group]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q5HRU2	3.43e-21	206	349	47	190	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
Q8CMN2	3.43e-21	206	349	47	190	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q49UX4	7.49e-19	244	349	88	193	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
Q2G0U9	6.21e-17	206	349	47	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=sle1 PE=1 SV=1
Q5HIL2	6.21e-17	206	349	47	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain COL) OX=93062 GN=sle1 PE=3 SV=1

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
1.000012	0.000025	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004417_00557.