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CAZyme Information: MGYG000003413_01728
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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 | Akkermansia sp900766865 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales; Akkermansiaceae; Akkermansia; Akkermansia sp900766865 | |||||||||||
| CAZyme ID | MGYG000003413_01728 | |||||||||||
| CAZy Family | GT28 | |||||||||||
| CAZyme Description | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1747; End: 2829 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT28 | 193 | 349 | 8.5e-47 | 0.9872611464968153 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03785 | GT28_MurG | 5.14e-114 | 7 | 348 | 2 | 342 | undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. |
| PRK00726 | murG | 3.27e-112 | 1 | 348 | 1 | 342 | undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
| COG0707 | MurG | 2.11e-94 | 7 | 348 | 3 | 342 | UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]. |
| TIGR01133 | murG | 7.78e-91 | 7 | 348 | 3 | 339 | undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan] |
| pfam04101 | Glyco_tran_28_C | 2.77e-34 | 192 | 348 | 1 | 161 | Glycosyltransferase family 28 C-terminal domain. The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| SEH81449.1 | 2.68e-145 | 3 | 357 | 5 | 359 |
| QWO90501.1 | 1.54e-129 | 2 | 357 | 8 | 364 |
| QWO94144.1 | 1.54e-129 | 2 | 357 | 8 | 364 |
| QWO96710.1 | 1.54e-129 | 2 | 357 | 8 | 364 |
| QWO86889.1 | 1.54e-129 | 2 | 357 | 8 | 364 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7D1I_A | 1.84e-50 | 2 | 349 | 7 | 354 | ChainA, UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase [Acinetobacter baumannii],7D1I_B Chain B, UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase [Acinetobacter baumannii],7D1I_C Chain C, UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase [Acinetobacter baumannii] |
| 3S2U_A | 2.05e-42 | 6 | 358 | 4 | 352 | Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1] |
| 1F0K_A | 8.17e-40 | 6 | 357 | 8 | 350 | The1.9 Angstrom Crystal Structure Of E. Coli Murg [Escherichia coli],1F0K_B The 1.9 Angstrom Crystal Structure Of E. Coli Murg [Escherichia coli],1NLM_A Crystal Structure Of Murg:glcnac Complex [Escherichia coli],1NLM_B Crystal Structure Of Murg:glcnac Complex [Escherichia coli] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q1D0T0 | 1.70e-57 | 5 | 354 | 2 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=murG PE=3 SV=1 |
| B5EBQ1 | 3.49e-57 | 5 | 358 | 1 | 355 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem) OX=404380 GN=murG PE=3 SV=1 |
| C6DZK6 | 6.88e-57 | 5 | 358 | 1 | 355 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Geobacter sp. (strain M21) OX=443144 GN=murG PE=3 SV=1 |
| B0K3H0 | 1.60e-56 | 5 | 353 | 1 | 356 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=murG PE=3 SV=1 |
| B0K8K7 | 1.60e-56 | 5 | 353 | 1 | 356 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=murG PE=3 SV=1 |
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 |
|---|---|---|---|---|---|
| 1.000061 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |