CAZyme Information: MGYG000002377_02404

Basic Information

• Species: Clostridium_X cadaveris
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_X; Clostridium_X cadaveris
• CAZyme ID: MGYG000002377_02404
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
364	MGYG000002377_15|CGC1	40515.65	4.2323

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002377	3460249	Isolate	not provided	not provided

• Gene Location: Start: 86712; End: 87806 Strand: +

Full Sequence      

MQSRNAGTYNGIDISSWEGNVNFSGVRSDGIDIVYIKATEGTGYINPYMNSTYNNARNND
LKIGFYHFFRANVDAREQARYFVENIGDKTSDCRLALDIETTEGYDAVTLTDMCVDFLEE
VKSLSGKEVVVYTYSNFAQTSLTSRLSSYPLWIAAYGVDTPSSNSIWDRWIGFQYSDTGR
VSGVNGNCDLDVFTEEIFLSLDVSSTGDQNSSGEEIIYTVKSGDTLSGIAHLYGTTWQNL
AEINHLSDPNLIYPGEKIVINHKSYEDIYIVKPGDTLSGIAQLYGTTWQHLAEINHLSNP
NLIYPGQSIDVGFENNNSETYVVKSGDTLSGIAQLYGTTWQHLAEINNLRDPNLIYPGEV
VNIR

Enzyme Prediction     

No EC number prediction in MGYG000002377_02404.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	12	184	1.5e-51	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	2.08e-87	10	193	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	5.91e-65	11	193	2	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.
pfam01183	Glyco_hydro_25	6.00e-58	12	184	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	2.30e-48	11	193	65	253	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06412	GH25_CH-type	1.87e-43	11	193	3	192	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM70433.1	2.71e-128	1	363	1	372
QAS60493.1	8.38e-123	1	363	1	384
AYE35100.1	8.38e-123	1	363	1	384
QBJ75914.1	2.91e-119	1	363	1	384
ATD56705.1	2.91e-119	1	363	1	384

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	2.58e-79	11	199	22	213	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	6.33e-78	11	225	22	253	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	8.13e-30	11	193	7	202	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	3.53e-22	13	196	26	204	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2WAG_A	5.82e-17	11	193	18	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	1.25e-74	1	197	1	200	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	9.02e-43	11	229	3	222	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	2.55e-28	11	193	84	279	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8X7H0	4.29e-27	8	196	66	259	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	1.15e-26	8	193	66	254	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2

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
1.000041	0.000019	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002377_02404.