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CAZyme Information: MGYG000002192_02014

You are here: Home > Sequence: MGYG000002192_02014

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 Acutalibacter sp900543305
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Acutalibacter; Acutalibacter sp900543305
CAZyme ID MGYG000002192_02014
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
290 32833.68 4.3997
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002192 2487718 MAG Spain Europe
Gene Location Start: 13796;  End: 14668  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002192_02014.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 9 180 4.1e-38 0.9887005649717514

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06414 GH25_LytC-like 3.24e-74 7 189 2 191
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.
cd00599 GH25_muramidase 2.10e-29 7 187 1 183
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 3.88e-18 7 186 1 180
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 3.38e-17 9 180 1 179
Glycosyl hydrolases family 25.
cd06524 GH25_YegX-like 4.20e-14 7 174 1 176
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQR28680.1 3.07e-122 1 281 1 279
ASB39388.1 1.15e-121 1 281 9 287
ANU53934.2 1.15e-121 1 281 9 287
QQR29472.1 8.28e-76 8 282 7 271
ASB40187.1 1.45e-75 8 282 25 289

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WW5_A 5.96e-22 2 180 265 457
3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A 1.50e-21 2 180 265 457
3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4JZ5_A 8.19e-08 9 175 26 197
High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
3HMC_A 1.64e-06 9 180 8 170
Endolysinfrom Bacillus anthracis [Bacillus anthracis]

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
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002192_02014.