CAZyme Information: MGYG000001490_01604

Basic Information

• Species: Bifidobacterium catenulatum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium catenulatum
• CAZyme ID: MGYG000001490_01604
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
604		67097.88	4.6192

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001490	2079525	Isolate	not provided	not provided

• Gene Location: Start: 1860466; End: 1862280 Strand: -

Full Sequence      

MVSPHHVLKIATALSAVALTASVAVTPAYALQDIAIEDAVAQRGAVTADNGVVMQSDDQS
DDQTGDQQSQDSMPDNPNAKLPGTVSDEISDDATVVSEDLAVTPEGEVKNIETGETVTDA
TLVGTQDQQPDPLAKTNGESFIPVSAEDVKNAVADANVQLSKFESNEYGAHWGTYNNTKA
FFDYQNNLFVQQAKGVIDVSEWQGDIDWAKAKADGVEGVIIRLGYGEGNNADKKAQRNIS
ECKRLGIPFGIYWYSYADTPSIAKEEGADVVAKLKQFGVNASDLAYPVYYDLEKWTWEGH
QPPTDPNVYNDIVNNWYSALQSAGYKNLSVYSYTSYLQGPLKHADIYAKTTWVAQYGARM
GFDSFPTDSRGWQYTSSGKVDGISGNVDMNAFGNKAYVNGGHWVTKNGQKYWWDSDGSLA
RSKEIYDPESNAWYWIDSDGTMAHDKDVYLRSNGGKWVRYDSNGHMIKGEDFRYGVWYNF
DFTTGAMSKGMTYLSNGNKWVYYDMVTGKMAHGEAYLNFDKEHSGWYLFDNITGARCTGD
IFIRANGGKWVRYDQKTGKMVKGLQKQNGLWYYFDPVTGAMAHGNTWVPQWQAWHYFDSV
TGRG

Enzyme Prediction     

No EC number prediction in MGYG000001490_01604.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	197	383	9.3e-39	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	5.61e-69	194	392	1	190	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	1.36e-27	196	392	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.
cd06523	GH25_PlyB-like	6.00e-24	196	391	2	176	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd06522	GH25_AtlA-like	4.16e-20	196	390	3	189	AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
cd06525	GH25_Lyc-like	3.37e-19	194	392	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAR02517.1	0.0	1	604	1	604
QTL81480.1	0.0	1	604	1	604
AVT45934.1	1.77e-279	1	604	1	603
AZH72073.1	8.30e-278	1	604	1	603
BAR04328.1	4.78e-264	1	397	1	397

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	6.88e-41	164	392	238	467	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	1.77e-40	164	392	238	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRU_A	9.50e-13	197	407	23	222	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.87e-12	197	407	23	222	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]
3HMC_A	4.70e-11	196	407	7	191	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.46e-11	197	392	12	196	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.09e-07	197	396	85	283	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8X7H0	2.18e-07	197	392	70	254	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P34020	7.37e-07	197	400	4	188	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
P76421	9.35e-07	197	392	70	254	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2

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
0.000280	0.999014	0.000170	0.000188	0.000165	0.000142

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001490_01604.