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CAZyme Information: MGYG000000155_01973

You are here: Home > Sequence: MGYG000000155_01973

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Weissella confusa
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Weissella; Weissella confusa
CAZyme ID MGYG000000155_01973
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
280 30614.99 4.3061
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000155 2346100 Isolate China Asia
Gene Location Start: 57407;  End: 58249  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000155_01973.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 6 182 2e-41 0.9887005649717514

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06417 GH25_LysA-like 6.84e-81 3 199 1 195
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
pfam01183 Glyco_hydro_25 2.00e-41 6 182 1 179
Glycosyl hydrolases family 25.
cd06525 GH25_Lyc-like 5.05e-39 4 192 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 1.72e-37 5 192 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.
cd06524 GH25_YegX-like 1.47e-28 5 194 2 194
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QIE78206.1 3.89e-181 1 280 1 280
QIL49850.1 2.42e-122 1 273 1 267
APS41325.1 4.39e-122 1 274 1 264
APS42173.1 1.60e-110 1 274 1 275
CBK80688.1 3.66e-80 1 205 1 208

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4KRU_A 1.29e-19 3 192 20 207
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A 7.30e-19 3 192 20 207
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 4.31e-14 3 194 5 204
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
6ZMV_A 1.31e-13 2 188 1 198
ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
2X8R_A 2.94e-11 3 79 4 85
Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26836 1.64e-14 3 209 9 214
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P00721 4.32e-14 3 188 2 203
N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1
P34020 1.24e-13 3 192 1 180
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 6.17e-13 3 194 82 281
Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
D4ANU4 2.82e-12 2 204 29 233
N,O-diacetylmuramidase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05911 PE=1 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
1.000080 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000155_01973.