CAZyme Information: MGYG000000244_01509

Basic Information

• Species: Catenibacterium sp000437715
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Catenibacterium; Catenibacterium sp000437715
• CAZyme ID: MGYG000000244_01509
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
280		31691.54	8.7508

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000244	2463343	Isolate	China	Asia

• Gene Location: Start: 8025; End: 8867 Strand: +

Full Sequence      

MSNYIIDISYHNGKVDLSKAKESISGVVARCSYGWSSGNIDKQWNNNARQANELGIPLFA
YHFCYARNEYEAKREAYLALQACRNYQVCIIYYDIEYSDYQGSLSNEMYYKIAKSFCDVI
EGAGYSAGIYANQDWFKNKLTNSGFSAWTLWIANYGLNNGYNNWDNKIQYNPFGNVLLHQ
FTSNAKKGALKDIKGIDSKFLDCSYDHGVISTFYKVKNKTSSLNVGDSVRVKTGSKWYDG
QSIANFVFKNQYEVIQVKGDRVVIGVNGKVTGAISLNSLY

Enzyme Prediction     

No EC number prediction in MGYG000000244_01509.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	186	1.9e-34	0.9717514124293786

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.69e-45	6	205	4	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	3.58e-20	4	189	1	176	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	2.29e-09	6	153	1	150	Glycosyl hydrolases family 25.
cd06522	GH25_AtlA-like	7.94e-08	3	185	1	177	AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
cd06524	GH25_YegX-like	1.23e-07	6	195	3	185	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL57292.1	4.60e-174	1	279	3	281
ASM70105.1	1.71e-27	1	160	1	156
QMW77121.1	1.50e-26	5	155	6	154
QIB54792.1	1.50e-26	5	155	6	154
QMW73604.1	3.37e-26	1	174	1	176

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	3.12e-06	5	225	24	220	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000037	0.000005	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000244_01509.