dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003355_04087

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Basic Information help

Species

Lachnoclostridium phytofermentans_A

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium; Lachnoclostridium phytofermentans_A

CAZyme ID

MGYG000003355_04087

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
628	MGYG000003355_180\|CGC1	71510.02	4.3601

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003355	5194070	MAG	China	Asia

Gene Location

Start: 32864; End: 34750 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003355_04087.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	426	608	4.3e-46	0.9943502824858758

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.86e-97	423	618	1	191	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	5.65e-40	424	616	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.
pfam01183	Glyco_hydro_25	1.86e-34	426	608	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	3.37e-32	423	615	3	187	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.
cd06525	GH25_Lyc-like	1.70e-30	425	615	2	182	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABX43465.1	0.0	1	628	1	628
QHI72152.1	2.51e-70	393	621	63	291
QNM03294.1	6.32e-69	389	621	146	380
BBF45127.1	1.39e-67	387	621	44	280
QRO38911.1	1.08e-65	385	621	50	288

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	5.41e-18	422	628	19	222	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.59e-17	422	628	19	222	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]
2WAG_A	1.03e-13	423	618	16	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
3HMC_A	5.86e-12	424	615	6	177	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
1JFX_A	4.15e-11	423	615	5	200	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	1.98e-13	422	615	8	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8FFY2	2.88e-13	422	616	66	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	3.88e-13	422	616	66	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	5.22e-13	422	616	66	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
P34020	3.27e-10	425	614	3	177	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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999867	0.000110	0.000009	0.000001	0.000000	0.000012

TMHMM Annotations download full data without filtering help

start	end
61	83