dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002309_02145

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Basic Information help

Species

Kurthia senegalensis

Lineage

Bacteria; Firmicutes; Bacilli; Bacillales_A; Planococcaceae; Kurthia; Kurthia senegalensis

CAZyme ID

MGYG000002309_02145

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
726		80099.43	9.8666

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002309	2976740	Isolate	Senegal	Africa

Gene Location

Start: 90678; End: 92858 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002309_02145.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	66	232	1.1e-41	0.9943502824858758

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06523	GH25_PlyB-like	4.64e-75	64	241	1	177	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd06414	GH25_LytC-like	6.64e-37	64	239	2	188	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	8.56e-31	64	239	1	184	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	9.09e-27	66	232	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	2.84e-23	66	241	6	189	Uncharacterized bacterial muramidase containing 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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOV12973.1	3.80e-140	25	495	25	484
QOV12974.1	5.73e-136	27	495	27	485
AMA61928.1	6.87e-124	29	496	35	493
VEI06850.1	1.64e-116	27	495	36	498
VEI06849.1	4.82e-110	32	497	32	490

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HMC_A	4.77e-46	65	248	7	186	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
2NW0_A	5.32e-44	65	255	3	188	ChainA, PlyB [Bacteriophage sp.],2NW0_B Chain B, PlyB [Bacteriophage sp.]
4JZ5_A	4.49e-24	65	239	25	210	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
2WAG_A	1.24e-13	64	255	17	220	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	9.10e-11	66	240	8	201	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.38e-13	60	264	6	217	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8FFY2	6.37e-13	66	260	70	271	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	8.58e-13	66	239	70	252	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	2.10e-12	66	239	70	252	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P25310	1.33e-09	66	240	85	278	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000250	0.999063	0.000165	0.000201	0.000168	0.000145

TMHMM Annotations help

There is no transmembrane helices in MGYG000002309_02145.