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CAZyme Information: MGYG000001339_01225

You are here: Home > Sequence: MGYG000001339_01225

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 Acetomicrobium hydrogeniformans
Lineage Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae; Acetomicrobium; Acetomicrobium hydrogeniformans
CAZyme ID MGYG000001339_01225
CAZy Family GH23
CAZyme Description Membrane-bound lytic murein transglycosylase F
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
184 MGYG000001339_1|CGC7 20965.92 8.3171
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001339 2123925 Isolate not provided North America
Gene Location Start: 1243132;  End: 1243686  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001339_01225.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH23 71 181 3.2e-32 0.8222222222222222

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00254 LT-like 3.33e-55 73 177 2 111
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.
cd16896 LT_Slt70-like 3.39e-42 58 178 5 146
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.
cd13401 Slt70-like 3.89e-39 59 172 8 142
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.
cd13403 MLTF-like 8.10e-38 61 181 1 161
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.
pfam01464 SLT 6.79e-35 65 168 5 114
Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AFM20926.1 1.59e-66 1 183 1 185
QCY19456.1 1.23e-47 41 176 42 179
QDD06091.1 1.23e-47 41 176 42 179
QCJ19437.1 1.23e-47 41 176 42 179
ADM37223.1 8.02e-47 41 176 106 243

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1QSA_A 6.74e-12 59 181 455 599
CrystalStructure Of The 70 Kda Soluble Lytic Transglycosylase Slt70 From Escherichia Coli At 1.65 Angstroms Resolution [Escherichia coli],1QTE_A Crystal Structure Of The 70 Kda Soluble Lytic Transglycosylase Slt70 From Escherichia Coli At 1.90 A Resolution In Complex With A 1,6- Anhydromurotripeptide [Escherichia coli]
6FBT_A 4.19e-11 72 172 464 585
ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa]
5OHU_A 4.24e-11 72 172 493 614
TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa]
5MPQ_A 1.03e-10 65 174 424 550
BulgecinA: The key to a broad-spectrum inhibitor that targets lytic transglycosylases [Neisseria meningitidis]
5O1J_A 1.03e-10 65 174 428 554
Lytictransglycosylase in action [Neisseria meningitidis MC58]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31608 2.28e-46 56 176 59 179
Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
O64046 2.59e-37 61 178 1426 1543
Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976 2.59e-37 61 178 1426 1543
SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
P27380 1.48e-18 65 155 15 104
Transglycosylase OS=Enterobacteria phage PRD1 OX=10658 GN=VII PE=1 SV=3
A8ZWR8 2.92e-12 60 153 289 388
Membrane-bound lytic murein transglycosylase F OS=Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3) OX=96561 GN=mltF 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
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001339_01225.