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CAZyme Information: MGYG000000224_01654

You are here: Home > Sequence: MGYG000000224_01654

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 Bacteroides sp003545565
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp003545565
CAZyme ID MGYG000000224_01654
CAZy Family GH23
CAZyme Description Membrane-bound lytic murein transglycosylase F
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
474 MGYG000000224_5|CGC2 53342.12 7.7256
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000224 3747034 Isolate China Asia
Gene Location Start: 164222;  End: 165646  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000224_01654.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH23 314 462 1.9e-22 0.7777777777777778

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10859 PRK10859 1.44e-97 19 461 9 443
membrane-bound lytic murein transglycosylase MltF.
COG4623 MltF 4.24e-88 41 461 9 424
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms].
cd13403 MLTF-like 3.60e-82 306 470 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.
cd01009 PBP2_YfhD_N 6.88e-76 55 281 1 223
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold protein superfamily. This subfamily includes the solute binding domain YfhD_N. These domains are found in the YfhD proteins that are predicted to function as lytic transglycosylases that cleave the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin in peptidoglycan, while the YfhD_N domain might act as an auxiliary or regulatory subunit. In addition to periplasmic solute binding domain, they have an SLT domain, typically found in soluble lytic transglycosylases, and a C-terminal low complexity domain. The YfhD proteins might have been recruited to create localized cell wall openings required for transport of large substrates such as DNA. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
cd00254 LT-like 3.61e-24 318 410 2 90
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT43782.1 0.0 1 474 1 474
QPH57788.1 4.06e-306 7 474 7 472
QRQ50382.1 7.50e-304 30 474 1 445
QUU00068.1 2.16e-303 8 473 8 472
QUT34267.1 8.79e-303 8 473 8 472

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4OWD_A 3.87e-45 39 466 2 426
Crystalstructure of MltF from Pseudomonas aeruginosa complexed with cysteine [Pseudomonas aeruginosa PAO1],4OXV_A Crystal structure of MltF from Pseudomonas aeruginosa complexed with valine [Pseudomonas aeruginosa PADK2_CF510],4P0G_A Crystal structure of MltF from Pseudomonas aeruginosa complexed with bulgecin and muropeptide [Pseudomonas aeruginosa PAO1],4P11_A Native crystal structure of MltF Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
4OZ9_A 1.25e-44 48 466 4 419
Crystalstructure of MltF from Pseudomonas aeruginosa complexed with isoleucine [Pseudomonas aeruginosa PAO1]
4OYV_A 5.32e-44 39 466 2 426
Crystalstructure of MltF from Pseudomonas aeruginosa complexed with leucine [Pseudomonas aeruginosa PAO1]
5AA3_A 6.33e-44 37 466 34 460
Crystalstructure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_B Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_C Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_D Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_E Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_F Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_G Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_H Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_I Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_J Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_K Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013],5AA3_L Crystal structure of MltF from Pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide [Pseudomonas aeruginosa BWHPSA013]
5AA2_A 6.33e-44 37 466 34 460
Crystalstructure of MltF from Pseudomonas aeruginosa in complex with NAM-pentapeptide. [Pseudomonas aeruginosa BWHPSA013],5AA2_C Crystal structure of MltF from Pseudomonas aeruginosa in complex with NAM-pentapeptide. [Pseudomonas aeruginosa BWHPSA013]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A8ZWR8 4.58e-58 48 471 34 451
Membrane-bound lytic murein transglycosylase F OS=Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3) OX=96561 GN=mltF PE=3 SV=2
Q5E750 1.27e-53 20 466 14 450
Membrane-bound lytic murein transglycosylase F OS=Aliivibrio fischeri (strain ATCC 700601 / ES114) OX=312309 GN=mltF PE=3 SV=2
A0KJ50 4.88e-53 10 466 7 451
Membrane-bound lytic murein transglycosylase F OS=Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049) OX=380703 GN=mltF PE=3 SV=1
A4SNZ5 1.32e-52 10 466 7 451
Membrane-bound lytic murein transglycosylase F OS=Aeromonas salmonicida (strain A449) OX=382245 GN=mltF PE=3 SV=1
Q47XX8 1.07e-50 37 466 18 440
Membrane-bound lytic murein transglycosylase F OS=Colwellia psychrerythraea (strain 34H / ATCC BAA-681) OX=167879 GN=mltF 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
0.106794 0.714406 0.177332 0.000789 0.000331 0.000317

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000224_01654.