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CAZyme Information: MGYG000002044_01123

You are here: Home > Sequence: MGYG000002044_01123

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 Fructilactobacillus sanfranciscensis
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Fructilactobacillus; Fructilactobacillus sanfranciscensis
CAZyme ID MGYG000002044_01123
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
265 MGYG000002044_69|CGC1 30610.76 9.9703
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002044 1209423 MAG China Asia
Gene Location Start: 2139;  End: 2936  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002044_01123.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 67 193 5e-19 0.6892655367231638

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06419 GH25_muramidase_2 1.20e-40 53 239 3 190
Uncharacterized bacterial muramidase containing 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 2.70e-22 59 189 1 127
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.
cd06413 GH25_muramidase_1 5.49e-18 57 184 2 129
Uncharacterized bacterial muramidase containing 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.
cd06525 GH25_Lyc-like 4.12e-14 59 148 1 86
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.
COG3757 Acm 5.51e-10 55 255 60 269
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QFX94256.1 3.21e-186 1 265 10 274
AEN99459.1 2.88e-129 62 245 1 184
ANZ57969.1 1.58e-117 1 265 1 265
ANZ59239.1 1.58e-117 1 265 1 265
QFX92440.1 1.50e-61 1 265 1 270

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WAG_A 1.39e-14 44 249 2 216
TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A 1.31e-06 58 116 5 63
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A 4.78e-06 58 149 20 110
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A 7.70e-06 58 149 20 110
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      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26836 5.09e-07 58 149 9 99
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020 2.11e-06 58 116 1 59
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

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
0.999971 0.000031 0.000000 0.000000 0.000000 0.000021

TMHMM  Annotations      download full data without filtering help

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21 43