CAZyme Information: MGYG000003683_01521

Basic Information

• Species: Bifidobacterium pseudocatenulatum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium pseudocatenulatum
• CAZyme ID: MGYG000003683_01521
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
669		74291.88	4.9058

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003683	2206268	Isolate	China	Asia

• Gene Location: Start: 7968; End: 9977 Strand: +

Full Sequence      

MVSPHHVVKIATALSAVALTASVAVAPAYALQDIAIEDAVAQSGSVTADNGVAMQSDNQS
DDQTGGQQSQDSMPDNPNAKLPDNVSDEISDDATVVSEDLAVTPEGEVKNIETGEIVTDP
TLVGTKDQQPDPLAKTNGESFIPVSAEDVKNAVVDANIQLSKFESNEYGAHWGTYNNSKA
FFDYQNNLFVQQAKGVIDVSGWQGDIDWAKAKADGVEGAIIRLGYGEGNNADKKAQRNIS
ECKRLGIPFGIYWYSYADTPALAKEEGADVVAKLKQFGVNPSDLAYPVYYDLEKWTWEGH
QPPTDPNVYNNIVNNWYSALQSAGYKNLGVYSYTSYLQGPLKHVDIYAKTTWVAQYGARM
GFDSFPTNSRGWQYTSTGKVDGISGNVDMNAFGNKEYVNGGSINSATSYEVKGNMGVEWR
SIGAEKSVIGKPIANEVCDWTQGRVNCYQNFENGAISWTPSTGAHYTTGAIRKEWARRNY
EHGVLGYPIEDEKKLSNDWKYQRFQNGDIWSRGTKESRIVLYNLRDSFYKNGGYSSLGGP
VADEESMGRGWWRQRFQYGDVWSKDGTNYRFVIKFDLRDSWNQHRGFSWLGAPVANEENM
GNGYWRQRCENGDVWTRNGASEKYIVMLNLRKEYYAKGGFSKLGGPVSEERNLGSIWRQD
FQKGSIYAH

Enzyme Prediction     

No EC number prediction in MGYG000003683_01521.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	197	383	6.2e-39	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	8.59e-70	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	1.43e-28	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	4.82e-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	1.13e-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.
COG3757	Acm	2.29e-19	176	399	45	260	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
BAR04328.1	1.74e-278	1	397	1	397
QTL81480.1	1.62e-275	1	401	1	401
BAR02517.1	5.65e-259	1	401	1	401
VEG16747.1	2.65e-257	1	404	1	404
ALE10489.1	2.65e-257	1	404	1	404

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.96e-38	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	4.94e-38	164	392	238	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
6SWZ_AAA	2.32e-15	395	623	23	250	ChainAAA, Protein PS1 [Corynebacterium glutamicum]
6SX4_AAA	3.13e-14	367	623	347	612	ChainAAA, Protein PS1 [Corynebacterium glutamicum],6SX4_BBB Chain BBB, Protein PS1 [Corynebacterium glutamicum],6SX4_CCC Chain CCC, Protein PS1 [Corynebacterium glutamicum],6SX4_DDD Chain DDD, Protein PS1 [Corynebacterium glutamicum]
4KRT_A	8.06e-12	197	436	23	252	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0C1D6	1.04e-13	367	623	390	655	Protein PS1 OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=csp1 PE=1 SV=1
P0C1D7	2.39e-13	367	623	390	655	Protein PS1 OS=Corynebacterium melassecola OX=41643 GN=csp1 PE=4 SV=1
P26836	2.30e-10	197	436	12	241	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.67e-07	197	392	85	279	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8X7H0	1.07e-06	197	396	70	258	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000267	0.999041	0.000167	0.000182	0.000163	0.000142

TMHMM  Annotations     

start	end
7	29