CAZyme Information: MGYG000000484_00589

Basic Information

• Species: Butyrivibrio_A sp000431815
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Butyrivibrio_A; Butyrivibrio_A sp000431815
• CAZyme ID: MGYG000000484_00589
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
315	MGYG000000484_2|CGC4	35008.27	9.3848

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000484	2428908	MAG	Fiji	Oceania

• Gene Location: Start: 264723; End: 265670 Strand: -

Full Sequence      

MSQRFGIDVSRWQGSFDFARAKSKEGVEFAIIKAGGADSGLYKDSQFEANYKKCVECRLP
KGAYFYGNARSTAEAKKEAGYFLSLLKGKKFEYPVFYDVEGSMITKNDRNTLTQIIKAFC
SEMEVAGCWAGIYSSESFFNSEMNDGELTRYTHWVARWGKNKPAPASGAETQIWQFGGET
NLIRSNKINGQTCDQDYCYVDFPAKIKAAGLNGYAKGNSSAPAKKSNEEIAAEVIAGKWG
NGTERQNRLSQAGYDYSAIQSIVNKKLSPSKKSVDEIAREVIHGDWGNGTKRKNRISAAG
YDYSAVQKRVNELLR

Enzyme Prediction     

No EC number prediction in MGYG000000484_00589.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	7	178	6.1e-40	0.9548022598870056

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	9.71e-71	4	199	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	2.35e-29	6	179	2	171	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	1.30e-23	7	176	1	171	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	2.52e-20	6	197	2	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.
pfam08230	CW_7	6.75e-19	275	314	1	40	CW_7 repeat. This domain was originally found in the C-terminal moiety of the Cpl-7 lysozyme encoded by the Streptococcus pneumoniae bacteriophage Cp-7. It is also found in the cell wall hydrolases of human and life-stock pathogens. CW_7 repeats make up a cell wall binding motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHB22110.1	4.78e-179	1	268	1	269
QEI32774.1	4.78e-179	1	268	1	269
ACR75820.1	5.53e-79	1	264	1	263
ARP51107.1	1.66e-72	6	267	5	264
ARP49658.1	9.20e-69	6	267	5	262

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	9.85e-15	6	190	7	204	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	2.85e-11	6	163	22	175	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	7.56e-11	6	163	22	175	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]
4CVD_A	1.91e-06	230	268	4	42	ChainA, LYSOZYME [Streptococcus phage CP-7]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	1.51e-13	6	190	84	281	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	8.98e-11	6	174	11	170	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P76421	4.56e-10	6	190	69	247	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	6.16e-10	6	190	69	247	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	6.16e-10	6	190	69	247	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 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
1.000055	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000484_00589.