CAZyme Information: MGYG000001554_02598

Basic Information

• Species: Corynebacterium phoceense
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium phoceense
• CAZyme ID: MGYG000001554_02598
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
464		50642.35	5.8513

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001554	2774100	Isolate	not provided	not provided

• Gene Location: Start: 1772520; End: 1773914 Strand: -

Full Sequence      

MTTMPVPKGFVVTSGFGPRWGRTHWGTDFGLAGGSGGQPIYAVRDGLITRAGSASGFGQW
ITLDVDAQHGGGLYVYGHIIPEVTVGQRVIEGQRIGHINPDSSTNGGVAPHLHFEHHRYV
WSQPGPDRLDPMQNVLAGAKWVGDSTKEEPMTTIFGVDVSEHQDGMSLAAAKAQGMDFAI
LRLCDGTYRDRTFRSHLADAESAGLLVSTYWYLRAPSEGSTIAQQVDVIDQQMGGRRDLG
VWIDVESVSGSRKLLTGADVWAAKRELEKRGYHVPGIYSGAWYWEQMPGGEPSMDGLGYL
WVSSYGRNRTGVPRDLYQGDGGDGHAGWSYPLGNRKPDLLQYGSNAHVAGRIVDINAFRG
TREQIAAIFNGDTQPQEELTVSEADRIIKHITDYISGFVGPIGSDTKDVRQQLTGGRDAG
DYRGWPQLGKDSQGRNLTVVDAIAALRVELAEFRAEFDKHVEEN

Enzyme Prediction     

No EC number prediction in MGYG000001554_02598.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	157	350	1.1e-29	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00599	GH25_muramidase	3.64e-23	156	358	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.
pfam01551	Peptidase_M23	2.67e-16	22	115	1	86	Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
pfam01183	Glyco_hydro_25	6.07e-16	157	330	1	171	Glycosyl hydrolases family 25.
cd12797	M23_peptidase	2.32e-15	24	115	1	84	M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
cd06414	GH25_LytC-like	1.44e-14	154	358	1	190	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ART22309.1	3.29e-224	4	382	1	388
ASE56543.1	1.71e-206	1	378	1	379
ALA67923.1	1.07e-202	1	378	1	379
QNE90250.1	1.52e-198	1	397	1	410
SQI23524.1	2.32e-197	1	415	1	433

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2X8R_A	2.54e-08	152	224	2	76	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O69731	1.17e-06	151	456	1	274	Uncharacterized protein Rv3766 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3766 PE=1 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
1.000033	0.000012	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001554_02598.