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CAZyme Information: MGYG000000572_01817

You are here: Home > Sequence: MGYG000000572_01817

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
Lineage Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Zag1;
CAZyme ID MGYG000000572_01817
CAZy Family GH23
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
229 25394.64 9.7901
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000572 1867050 MAG Madagascar Africa
Gene Location Start: 272;  End: 961  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000572_01817.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH23 57 165 2.8e-28 0.8222222222222222

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16896 LT_Slt70-like 2.43e-39 45 160 5 143
uncharacterized lytic transglycosylase subfamily with similarity to Slt70. Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has 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.
cd00254 LT-like 3.71e-39 59 159 1 108
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 5.23e-38 45 159 7 144
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.
cd16894 MltD-like 8.85e-27 69 158 17 125
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).
cd13403 MLTF-like 1.00e-26 48 144 1 105
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins. This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes 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, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AOR39353.1 3.88e-116 16 229 1 216
ADI02565.1 2.40e-29 54 163 102 212
AUW94962.1 1.06e-28 43 170 49 177
AQS60617.1 3.50e-28 37 158 79 202
AZT90545.1 6.28e-28 50 158 101 210

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5MPQ_A 8.75e-13 41 160 413 551
BulgecinA: The key to a broad-spectrum inhibitor that targets lytic transglycosylases [Neisseria meningitidis]
5O1J_A 8.78e-13 41 160 417 555
Lytictransglycosylase in action [Neisseria meningitidis MC58]
6FPN_B 8.81e-13 41 160 423 561
Lytictransglycosylase in action [Neisseria meningitidis MC58]
5O24_A 8.83e-13 41 160 427 565
Lytictransglycosylase in action [Neisseria meningitidis]
5O29_A 8.86e-13 41 160 433 571
Lytictransglycosylase in action [Neisseria meningitidis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31608 6.46e-25 43 157 59 175
Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
O31976 9.09e-23 52 163 1430 1543
SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
O64046 9.09e-23 52 163 1430 1543
Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
P27380 4.58e-09 47 173 10 131
Transglycosylase OS=Enterobacteria phage PRD1 OX=10658 GN=VII PE=1 SV=3

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
0.005787 0.874372 0.118698 0.000524 0.000316 0.000292

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000572_01817.