dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000062_01275

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Basic Information help

Species

Intestinibacter bartlettii

Lineage

Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Intestinibacter; Intestinibacter bartlettii

CAZyme ID

MGYG000000062_01275

CAZy Family

GH25

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
454	MGYG000000062_1\|CGC7	51075.31	4.8109

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000062	3140386	Isolate	United Kingdom	Europe

Gene Location

Start: 1331619; End: 1332983 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000062_01275.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH25	7	184	3.6e-50	0.9943502824858758

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	4.24e-88	5	191	1	182	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.
pfam01183	Glyco_hydro_25	4.03e-57	7	184	1	180	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	2.94e-54	5	192	1	185	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.
cd06524	GH25_YegX-like	9.54e-46	5	196	1	194	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.
cd06414	GH25_LytC-like	2.05e-40	5	194	2	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBJ75914.1	2.99e-119	5	454	10	442
ATD56705.1	2.99e-119	5	454	10	442
SLK20760.1	2.99e-119	5	454	10	442
ATD55618.1	2.99e-119	5	454	10	442
QAS60493.1	1.02e-110	5	395	10	384

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	7.56e-49	5	200	21	214	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.12e-47	5	200	21	214	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	3.13e-20	5	189	6	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4B8V_A	5.38e-20	229	391	42	212	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]
2WAG_A	1.67e-15	5	194	17	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	6.12e-48	5	190	10	193	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.30e-34	5	199	2	186	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	4.73e-24	2	193	63	254	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	4.73e-24	2	193	63	254	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q49UX4	6.02e-23	289	454	27	193	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 help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000062_01275.