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CAZyme Information: MGYG000003451_01520

You are here: Home > Sequence: MGYG000003451_01520

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
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Oxalobacter;
CAZyme ID MGYG000003451_01520
CAZy Family GH24
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
162 17233.78 9.5368
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003451 1832891 MAG Fiji Oceania
Gene Location Start: 2959;  End: 3447  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003451_01520.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH24 13 145 5.2e-50 0.9927007299270073

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16901 lyz_P1 1.14e-60 20 149 9 139
P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd00737 lyz_endolysin_autolysin 6.24e-58 21 148 5 134
endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd16900 endolysin_R21-like 1.28e-56 21 149 12 141
endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
COG3772 RrrD 1.04e-42 21 149 15 147
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
pfam00959 Phage_lysozyme 9.39e-14 38 143 1 107
Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ARQ46661.1 2.78e-73 2 151 3 152
QDX34129.1 3.62e-73 2 151 11 160
ARQ78370.1 2.35e-72 2 151 4 153
ARQ46250.1 2.35e-72 2 151 4 153
QDX34161.1 3.07e-72 2 151 12 161

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6ET6_A 3.12e-33 21 148 60 192
ChainA, Lysozyme [Acinetobacter baumannii]
7M5I_A 1.18e-21 25 145 21 149
ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
4ZPU_A 1.32e-20 10 149 17 160
Thestructure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_B The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_C The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_D The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12]
3HDE_A 1.47e-20 10 149 17 160
ChainA, Lysozyme [Enterobacteria phage P21],3HDE_B Chain B, Lysozyme [Enterobacteria phage P21],3HDE_C Chain C, Lysozyme [Enterobacteria phage P21],3HDE_D Chain D, Lysozyme [Enterobacteria phage P21]
3HDF_A 1.76e-19 32 149 17 135
ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9T1T5 3.66e-26 13 148 3 142
Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
O80292 1.52e-20 25 149 37 162
SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
P27359 2.05e-20 10 149 17 160
SAR-endolysin OS=Enterobacteria phage P21 OX=10711 GN=R PE=1 SV=1
P78285 5.72e-20 10 149 17 160
Lysozyme RrrD OS=Escherichia coli (strain K12) OX=83333 GN=rrrD PE=1 SV=1
Q7Y2C0 1.42e-19 12 154 8 153
SAR-endolysin OS=Pseudomonas phage phiKMV OX=204270 GN=45 PE=1 SV=1

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
0.275955 0.713188 0.010047 0.000287 0.000243 0.000268

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003451_01520.