CAZyme Information: MGYG000002827_03541

Basic Information

• Species: Phyllobacterium sp900539805
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales_A; Rhizobiaceae_A; Phyllobacterium; Phyllobacterium sp900539805
• CAZyme ID: MGYG000002827_03541
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
275	MGYG000002827_32|CGC1	31167.25	9.4021

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002827	5102924	MAG	Singapore	Asia

• Gene Location: Start: 1523; End: 2350 Strand: +

Full Sequence      

MKRLAAGLLTLLLAGCTTVDYDFSDAKKRASPAPLQQIAAPAGKINAPRFNDSNPHDWKG
RTPWHYPVHGTDVSKYQSTIDWAAVRGNRISFVFIKATEGADRVDDRLADNWQAARAAGI
PRGAYHFYYFCRTAKEQAQWFIRNVPNDPGALPPVLDMEWNAASPTCKLRPNAAVVRSEM
RVFIDILERHYGKRPIIYTTVDFFDDNDLRQLAGYPFWLRSVAGHPDEKYGPHPWTFWQY
TGTGSIPGIRGDADINVFAGDETAWKQWLVRNKVR

Enzyme Prediction     

No EC number prediction in MGYG000002827_03541.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	72	249	3.2e-56	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	2.84e-113	66	260	1	191	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.
COG3757	Acm	7.50e-94	48	269	42	264	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd00599	GH25_muramidase	3.62e-69	69	258	1	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.
pfam01183	Glyco_hydro_25	6.37e-66	72	249	2	180	Glycosyl hydrolases family 25.
cd06524	GH25_YegX-like	2.75e-57	69	260	1	194	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
QND53668.1	9.53e-197	1	275	1	272
ATU91014.1	7.73e-187	1	275	1	272
ABS14442.1	1.91e-163	1	275	1	277
AIK43428.1	1.91e-163	1	275	1	277
QNQ39887.1	5.48e-163	1	275	1	277

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.02e-44	66	272	14	220	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	1.19e-30	68	260	5	204	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	3.17e-21	70	258	22	207	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.05e-20	70	258	22	207	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]
2X8R_A	3.96e-16	68	239	4	183	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
Q8FFY2	1.00e-37	61	260	60	256	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	1.41e-37	61	260	60	256	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	2.78e-37	63	262	62	258	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P25310	3.73e-29	68	260	82	281	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	9.96e-20	70	258	11	196	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000070	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002827_03541.