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CAZyme Information: MGYG000001100_00865

You are here: Home > Sequence: MGYG000001100_00865

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 viridescens
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Weissella; Weissella viridescens
CAZyme ID MGYG000001100_00865
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
364 41479.42 9.4287
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001100 1591687 MAG China Asia
Gene Location Start: 1;  End: 1095  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001100_00865.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 33 220 2.1e-29 0.96045197740113

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00599 GH25_muramidase 1.16e-22 33 232 4 184
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.
cd06525 GH25_Lyc-like 3.61e-19 33 220 4 170
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 9.78e-19 33 220 2 175
Glycosyl hydrolases family 25.
cd06414 GH25_LytC-like 2.06e-15 33 228 5 191
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.
cd06417 GH25_LysA-like 8.08e-11 33 230 5 191
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QOD85769.1 1.88e-165 1 363 1 360
QEA44166.1 6.88e-56 8 364 14 367
QQB26664.1 8.73e-56 20 364 20 363
ADP69243.1 8.73e-56 20 364 20 363
QEA48077.1 1.05e-54 8 364 14 367

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4KRU_A 1.81e-10 33 225 24 205
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A 4.80e-10 33 225 24 205
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 1.57e-07 31 213 7 176
Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000271 0.998956 0.000213 0.000187 0.000178 0.000152

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001100_00865.