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CAZyme Information: MGYG000001493_05890

You are here: Home > Sequence: MGYG000001493_05890

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 Enterocloster bolteae
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster bolteae
CAZyme ID MGYG000001493_05890
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
367 MGYG000001493_11|CGC2 39779.39 5.2091
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001493 6583702 Isolate not provided not provided
Gene Location Start: 53045;  End: 54148  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001493_05890.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 110 284 1.1e-39 0.9830508474576272

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06414 GH25_LytC-like 4.63e-82 106 294 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 1.40e-26 106 288 1 181
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.
pfam01183 Glyco_hydro_25 2.67e-23 108 284 1 180
Glycosyl hydrolases family 25.
cd06525 GH25_Lyc-like 5.84e-19 106 288 1 179
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.
cd06413 GH25_muramidase_1 1.39e-18 106 288 4 184
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASN93256.1 7.86e-220 1 367 1 367
QRP42084.1 7.86e-220 1 367 1 367
QJU22303.1 4.92e-213 1 367 1 373
ADL03867.1 1.12e-141 57 349 7 301
QRV22095.1 1.12e-141 57 349 7 301

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8X7H0 3.90e-09 107 292 69 253
Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421 5.25e-09 107 292 69 253
Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2 7.05e-09 107 292 69 253
Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2

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
0.998677 0.001252 0.000054 0.000005 0.000003 0.000006

TMHMM  Annotations      download full data without filtering help

start end
60 82