logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004667_02222

You are here: Home > Sequence: MGYG000004667_02222

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 Clostridium beijerinckii
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium beijerinckii
CAZyme ID MGYG000004667_02222
CAZy Family GH24
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
284 32239.28 4.5157
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004667 6180974 Isolate United States North America
Gene Location Start: 26012;  End: 26866  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004667_02222.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH24 132 268 1.2e-31 0.9927007299270073

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00737 lyz_endolysin_autolysin 5.51e-44 136 272 1 135
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 1.25e-25 132 272 7 147
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
COG3409 PGRP 8.03e-22 4 120 40 184
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis].
cd16901 lyz_P1 1.33e-19 132 268 2 135
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.
pfam01471 PG_binding_1 3.20e-12 8 64 1 57
Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUN37948.1 5.28e-181 1 284 1 284
AQS01884.1 1.71e-46 1 279 1 289
AQS11484.1 1.71e-46 1 279 1 289
AQS15867.1 1.71e-46 1 279 1 289
AQR91982.1 1.71e-46 1 279 1 289

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7M5I_A 6.46e-11 132 279 9 160
ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
6ET6_A 1.19e-10 133 265 53 186
ChainA, Lysozyme [Acinetobacter baumannii]
6H9D_A 5.31e-08 132 234 6 105
ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
3BKH_A 2.70e-07 2 67 11 76
ChainA, lytic transglycosylase [Pseudomonas phage phiKZ],3BKV_A Chain A, lytic transglycosylase [Pseudomonas phage phiKZ]
2ANV_A 9.79e-06 132 265 4 138
ChainA, Lysozyme [Lederbergvirus P22],2ANV_B Chain B, Lysozyme [Lederbergvirus P22],2ANX_A Chain A, Lysozyme [Lederbergvirus P22],2ANX_B Chain B, Lysozyme [Lederbergvirus P22]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q37896 2.03e-20 132 283 3 153
Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P07540 1.23e-17 132 275 3 145
Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
P11187 1.23e-17 132 275 3 145
Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
Q9T1T5 1.95e-10 132 275 3 146
Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 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
1.000057 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004667_02222.