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CAZyme Information: MGYG000001898_01999

You are here: Home > Sequence: MGYG000001898_01999

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 Parabacteroides sp900552415
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900552415
CAZyme ID MGYG000001898_01999
CAZy Family GH23
CAZyme Description Membrane-bound lytic murein transglycosylase D
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
508 57387.61 6.8643
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001898 3107743 MAG Denmark Europe
Gene Location Start: 11261;  End: 12787  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001898_01999.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH23 130 263 4.3e-23 0.8666666666666667

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16894 MltD-like 5.96e-69 138 266 1 129
Membrane-bound lytic murein transglycosylase D and similar proteins. Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
PRK10783 mltD 9.43e-58 133 500 108 441
membrane-bound lytic murein transglycosylase D; Provisional
pfam01464 SLT 2.70e-30 133 246 1 114
Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
cd00254 LT-like 2.97e-19 153 266 10 110
lytic transglycosylase(LT)-like domain. Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
cd13401 Slt70-like 3.95e-19 130 258 6 139
70kDa soluble lytic transglycosylase (Slt70) and similar proteins. Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QJE29305.1 3.50e-282 1 508 1 515
BBK92552.1 1.43e-280 1 508 1 511
QUR47840.1 1.43e-280 1 508 1 511
QIX64548.1 1.43e-280 1 508 1 511
ABR44275.1 7.14e-278 1 508 1 518

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4UZ2_A 5.97e-06 459 506 1 47
Crystalstructure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_D Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ3_A Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0AEZ7 5.61e-37 99 505 71 442
Membrane-bound lytic murein transglycosylase D OS=Escherichia coli (strain K12) OX=83333 GN=mltD PE=1 SV=1
P0AEZ8 5.61e-37 99 505 71 442
Membrane-bound lytic murein transglycosylase D OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mltD PE=3 SV=1
O31608 4.62e-07 134 257 64 179
Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
Q8CMN2 1.01e-06 367 508 71 193
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2 1.01e-06 367 508 71 193
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1

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
0.000551 0.998361 0.000526 0.000186 0.000182 0.000169

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001898_01999.