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CAZyme Information: MGYG000002827_03359

You are here: Home > Sequence: MGYG000002827_03359

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 Phyllobacterium sp900539805
Lineage Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales_A; Rhizobiaceae_A; Phyllobacterium; Phyllobacterium sp900539805
CAZyme ID MGYG000002827_03359
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
416 46101.45 6.3427
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002827 5102924 MAG Singapore Asia
Gene Location Start: 59461;  End: 60711  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002827_03359.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 104 239 1.5e-22 0.7627118644067796

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3757 Acm 1.62e-34 101 274 14 181
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd00599 GH25_muramidase 3.64e-31 56 261 17 186
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.
cd06412 GH25_CH-type 1.62e-14 111 236 48 181
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.
pfam01183 Glyco_hydro_25 2.88e-14 103 237 37 174
Glycosyl hydrolases family 25.
cd06524 GH25_YegX-like 6.45e-14 48 234 13 174
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
QND52192.1 1.88e-232 1 412 31 441
AWC25094.1 1.22e-110 8 315 24 314
QNH33753.1 2.70e-110 9 278 26 294
QOF72959.1 2.70e-110 9 278 26 294
AMS43776.1 2.70e-110 9 278 26 294

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000262 0.999001 0.000222 0.000189 0.000158 0.000134

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002827_03359.