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CAZyme Information: MGYG000001317_00797

You are here: Home > Sequence: MGYG000001317_00797

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 Citrobacter portucalensis_A
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter portucalensis_A
CAZyme ID MGYG000001317_00797
CAZy Family GH24
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
116 MGYG000001317_7|CGC2 13285.24 5.1097
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001317 5150259 Isolate not provided not provided
Gene Location Start: 189033;  End: 189383  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001317_00797.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH24 11 104 8.8e-20 0.6934306569343066

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00737 lyz_endolysin_autolysin 7.28e-25 12 103 1 92
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.
COG3772 RrrD 4.01e-16 10 112 9 120
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900 endolysin_R21-like 3.60e-08 13 102 9 99
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.
cd16901 lyz_P1 2.08e-07 10 106 4 99
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.
cd00735 T4-like_lys 4.15e-06 20 99 10 96
bacteriophage T4-like lysozymes. Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AYL68120.1 7.98e-67 1 107 1 107
QET68457.1 7.98e-67 1 107 1 107
BBV28722.1 1.61e-66 1 107 1 107
BBV33736.1 1.61e-66 1 107 1 107
AWS94741.1 1.61e-66 1 107 1 107

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4EVX_A 7.17e-32 5 100 4 98
Crystalstructure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],4EVX_B Crystal structure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
6H9D_A 5.12e-08 4 105 1 101
ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
7M5I_A 2.26e-07 16 98 17 101
ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]

Swiss-Prot Hits      help

has no Swissprot hit.

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 MGYG000001317_00797.