CAZyme Information: MGYG000002018_00664

Basic Information

• Species: Anaerobutyricum sp900754855
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerobutyricum; Anaerobutyricum sp900754855
• CAZyme ID: MGYG000002018_00664
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
366	MGYG000002018_17|CGC1	41376.67	10.2542

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002018	2177164	MAG	Spain	Europe

• Gene Location: Start: 19386; End: 20486 Strand: -

Full Sequence      

MRFAFMKKMSVSCMLVMLGFFCLYTGVEAEEKNDRAESFRYVNGKEKESPPVFGVMNVNA
WKRDGDAFYNNRGQAIPGAYAMGIDVSSNNGSIDWNAVKADGVEFAIIRCGYGMNQPEQD
DKRWQENVAGCEAAGIPYGVYLYSYADSVSRAVSEAEHVLRLVAGRSLAYPVYFDMEDQS
IFRNTTAKQRVKIAEAFCKKIEAAGYKAAIYANHYAFTNELPEKNFNRWGRWVAHYAPKC
GYKGKYQMWQATNQGRIAGIQGNVDVNFMISDLAAEKPVIHVVSAGKKKVKVSWKPKKKG
TTCQIYYSRTKKEKGKLVTKNAGKGWAKIRKLKSGKTYYFRVRLSRKINGVTVCSKYSKS
RKLKVR

Enzyme Prediction     

No EC number prediction in MGYG000002018_00664.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	84	260	1.6e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.49e-91	83	268	3	189	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	2.25e-38	83	267	2	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.
cd06413	GH25_muramidase_1	1.81e-25	83	267	5	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.
pfam01183	Glyco_hydro_25	7.98e-24	84	260	1	180	Glycosyl hydrolases family 25.
cd06524	GH25_YegX-like	1.07e-22	83	267	2	190	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
SOB72005.1	2.40e-109	5	364	6	360
QUF79171.1	1.30e-82	29	259	28	259
QCP36075.1	7.80e-75	27	276	37	292
AWY97591.1	2.18e-74	27	271	38	286
QCP36076.1	1.22e-72	28	359	36	393

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.96e-22	56	267	242	465	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	4.89e-22	56	267	242	465	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
5A6S_A	1.44e-10	85	272	26	204	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
4KRT_A	4.93e-09	83	302	22	240	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	6.08e-09	83	267	18	204	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	1.65e-10	83	267	3	178	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
P25310	1.19e-06	82	267	83	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.007581	0.966142	0.025422	0.000352	0.000235	0.000225

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002018_00664.