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CAZyme Information: MGYG000001513_01362

You are here: Home > Sequence: MGYG000001513_01362

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_P massiliamazoniense
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_P; Clostridium_P massiliamazoniense
CAZyme ID MGYG000001513_01362
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
316 MGYG000001513_10|CGC2 35217.82 6.2637
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001513 3732600 Isolate not provided not provided
Gene Location Start: 562182;  End: 563132  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.17

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 5 174 9.9e-51 0.9943502824858758

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06525 GH25_Lyc-like 2.25e-72 3 184 1 184
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.
cd00599 GH25_muramidase 1.12e-53 3 184 1 186
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.
pfam01183 Glyco_hydro_25 6.58e-49 5 174 1 180
Glycosyl hydrolases family 25.
COG3757 Acm 2.11e-45 2 184 63 253
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06413 GH25_muramidase_1 8.49e-43 2 184 3 189
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
CDM70433.1 7.77e-69 2 315 9 319
QBJ75914.1 4.05e-67 2 315 9 324
ATD56705.1 4.05e-67 2 315 9 324
SLK20760.1 4.05e-67 2 315 9 324
ATD55618.1 4.05e-67 2 315 9 324

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4KRU_A 1.30e-64 2 207 20 227
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A 1.27e-63 2 250 20 275
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]
1JFX_A 1.74e-28 2 184 5 202
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A 4.68e-24 1 207 21 222
Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2WAG_A 1.31e-17 2 173 16 193
TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26836 4.49e-61 2 193 9 205
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020 7.84e-54 2 191 1 187
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 5.14e-27 2 184 82 279
Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8X7H0 2.39e-23 2 187 67 259
Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421 4.59e-23 2 184 67 254
Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 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
1.000036 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001513_01362.