CAZyme Information: MGYG000000390_01250

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae
• CAZyme ID: MGYG000000390_01250
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
442		47914.52	7.7767

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000390	2232010	MAG	Sweden	Europe

• Gene Location: Start: 4614; End: 5942 Strand: +

Full Sequence      

MLLFSIPMAMALPPSGGTIYQGIDVSQWQGKIDFAAVKSAGIQVVYIRSSLGGDYTDPMF
RQNYENAKAQGLKVGFYHYVTASNADQARQEAHFFASVVKGTAPDCRLAMDFEYLRGLTN
PEINQIALAFLRELEALTGRTPAVYTDTYMAANVYTKDLAAYPLWVAQWGASQPADNKVW
SSWSGFQYSSQGRVPGISGEVDLNRFTDGIFDPQSGELPDPGEPDPSGCTIVTYTVRTGD
TLSSIAAQYHTTAAEIAQLNKLPNPDLIFTGQKLLLCVDLDPGTGSYTVVYTVRTGDTLS
SIAARYHTTVASIVKLNQIKNPDLIYTGQKLTIQVTGVKPPQPSTVLYTVRAGDTLAAIA
ARYRTTVASIVTLNGIKNPDLIYAGQVFRIQPGASSRQVVVKTGDTLWGIAVKNRTTVTA
LAALNHIAPPYYIFTGQIIKLP

Enzyme Prediction     

No EC number prediction in MGYG000000390_01250.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	23	197	9.6e-53	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	7.73e-78	21	206	1	184	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.
cd00599	GH25_muramidase	6.76e-57	21	206	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.
cd06414	GH25_LytC-like	5.88e-55	21	204	2	188	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.
pfam01183	Glyco_hydro_25	6.41e-55	23	197	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	2.82e-47	18	211	61	258	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT55024.1	4.78e-140	9	442	25	466
QJS18123.1	7.67e-132	9	441	22	450
QIB56830.1	7.34e-115	1	390	15	402
QMW80393.1	7.34e-115	1	390	15	402
QBE96304.1	4.73e-113	1	390	15	402

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.96e-50	21	211	21	212	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	5.74e-49	21	211	21	212	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]
1JFX_A	7.20e-29	21	206	6	202	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	4.92e-26	12	217	14	212	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
4B8V_A	8.22e-19	232	386	42	212	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	7.88e-51	21	212	10	202	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.05e-33	21	211	2	185	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	8.59e-28	7	206	69	279	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P37710	2.63e-26	234	441	499	736	Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2
Q49UX4	3.03e-21	233	396	28	199	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

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
0.002141	0.996925	0.000216	0.000273	0.000230	0.000213

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000390_01250.