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CAZyme Information: MGYG000000295_01900

You are here: Home > Sequence: MGYG000000295_01900

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_E sporosphaeroides
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Clostridium_E; Clostridium_E sporosphaeroides
CAZyme ID MGYG000000295_01900
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
518 55578.74 8.6605
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000295 2812533 MAG Sweden Europe
Gene Location Start: 6226;  End: 7782  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000295_01900.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 139 310 8.6e-46 0.96045197740113

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06414 GH25_LytC-like 3.68e-80 136 325 1 191
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 2.38e-43 138 323 2 185
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 7.99e-35 138 323 2 183
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.
COG3757 Acm 8.17e-32 136 323 63 252
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
pfam01183 Glyco_hydro_25 1.62e-30 139 315 1 180
Glycosyl hydrolases family 25.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CAB1251277.1 2.32e-177 23 517 12 505
QAT49444.1 6.43e-109 23 518 33 628
QEY33648.1 1.46e-106 23 518 20 516
QNK41523.1 1.13e-104 27 414 1 388
QEY35154.1 4.36e-78 21 400 34 408

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4KRU_A 1.87e-17 136 322 20 205
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A 2.01e-17 135 334 4 208
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRT_A 1.10e-16 136 322 20 205
X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P34020 5.55e-20 138 344 3 202
Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P25310 4.05e-16 135 334 81 285
Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836 8.28e-13 136 322 9 194
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

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
0.141054 0.850345 0.007597 0.000382 0.000287 0.000331

TMHMM  Annotations      download full data without filtering help

start end
31 53