CAZyme Information: MGYG000001443_04017

Basic Information

• Species: Streptomyces albus
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Streptomycetales; Streptomycetaceae; Streptomyces; Streptomyces albus
• CAZyme ID: MGYG000001443_04017
• CAZy Family: GH25
• CAZyme Description: Lysozyme M1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
189		21800.62	9.5563

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001443	7820353	Isolate	not provided	not provided

• Gene Location: Start: 1835854; End: 1836423 Strand: +

Full Sequence      

MIKGIDVSSYQPSDYSTRGIEFVFIKLTEGKSYTNPKWVAQRKTARDAGLVTGFYHFVRP
GSMKKQADYFLSKIKLAPGDMLVLDWEDPKVSNDEKDDWIKYVQDKAPKHKVLLYCNRDF
WLNRDKTSFAGDGLWIAHYNGKPGEPGIKHRWRFHQYTSDPIDTNLGEFDSREALRSWAG
GRKKSAEGE

Enzyme Prediction     

No EC number prediction in MGYG000001443_04017.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	5	160	1.4e-40	0.96045197740113

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01183	Glyco_hydro_25	7.50e-44	5	162	1	176	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	1.14e-43	3	166	1	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.
cd06524	GH25_YegX-like	6.78e-30	3	158	1	175	YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.
cd06412	GH25_CH-type	4.93e-26	2	166	1	191	CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.
cd06525	GH25_Lyc-like	1.53e-25	3	159	1	168	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
QID39057.1	2.58e-143	1	189	1	189
QNF54222.1	1.89e-126	1	184	1	184
QHF95928.1	1.10e-125	1	184	1	184
QPP05646.1	2.81e-105	1	178	2	179
QNF57468.1	4.51e-99	2	179	5	182

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZMV_A	1.80e-11	2	175	2	203	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
4KRU_A	2.23e-10	2	160	20	192	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	4.35e-10	2	160	20	192	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]
2X8R_A	9.45e-07	2	156	4	183	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]
6ZM8_A	1.73e-06	2	72	2	78	ChainA, muramidase [Sodiomyces alcalophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.98e-10	2	158	9	179	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P00721	1.99e-10	2	121	2	144	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1
P34020	1.39e-08	2	158	1	163	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
D4ANU4	2.76e-07	2	157	30	205	N,O-diacetylmuramidase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05911 PE=1 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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001443_04017.