CAZyme Information: MGYG000000913_01032

Basic Information

• Species: Blautia sp900556555
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp900556555
• CAZyme ID: MGYG000000913_01032
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
356	MGYG000000913_27|CGC1	38845.91	9.6911

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000913	2138636	MAG	China	Asia

• Gene Location: Start: 1190; End: 2260 Strand: +

Full Sequence      

MSMNGIDISSWQKGINLNVVPCDFVIVKATGGTGYVNLDYTRAMQQAINAGKKVGVYHYA
RERGCKGSAIAEADFFVKTVQSYIGKAILVLDWEEELTLGVAWAKEFLDRVYQKTGVKAF
IYTSASVTRQYNWTSVAQAGYPLWMAQYPNNKPQNGYRDKPWTDGKGYGAFKTLAIHQYS
SSGRLPGYNGNLDVNKAYMDAAAWDKYAGTAEEKPTPAPIPSPAPSGTTLDLAAAVMQGK
YGAGQDRKNALGTRYQEVQDFINHIASASTDTLVAEVMQGKYGNGETRKTVLGGRYKAVQ
DKIDEKGSGAVYYTVRSGDTLSGIAAKYGTTYQKLAQMNGIANPNKIYAGQKIRVK

Enzyme Prediction     

No EC number prediction in MGYG000000913_01032.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	187	2.8e-44	0.9887005649717514
CBM50	313	355	1.3e-16	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	6.44e-80	3	204	1	195	LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
pfam01183	Glyco_hydro_25	2.41e-43	6	187	1	179	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	5.85e-42	5	197	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.
cd06525	GH25_Lyc-like	2.25e-32	4	196	1	183	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.
cd06524	GH25_YegX-like	3.81e-26	5	196	2	191	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
CBK80688.1	2.18e-115	1	356	1	362
QRT50187.1	2.60e-101	1	356	1	396
QRT50341.1	3.56e-89	1	356	1	346
QOP65129.1	1.79e-79	1	356	1	340
BBP07345.1	2.97e-77	1	217	1	214

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	1.98e-14	3	202	5	207	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	1.54e-13	2	196	19	206	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	5.37e-13	2	196	19	206	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]
6ZMV_A	1.35e-07	5	197	4	202	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
2X8R_A	2.56e-07	2	163	3	180	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
P25310	3.07e-13	3	202	82	284	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q49UX4	1.57e-10	313	355	88	129	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
Q8CMN2	5.37e-08	308	355	82	127	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2	5.37e-08	308	355	82	127	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
P00721	7.01e-08	2	126	1	142	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1

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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000913_01032.