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CAZyme Information: MGYG000001747_01297
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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 | UMGS743 sp900545085 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Christensenellaceae; UMGS743; UMGS743 sp900545085 | |||||||||||
| CAZyme ID | MGYG000001747_01297 | |||||||||||
| 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: 29768; End: 30859 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT28 | 188 | 333 | 4.1e-38 | 0.9171974522292994 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK12446 | PRK12446 | 1.35e-135 | 2 | 333 | 1 | 333 | undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
| PRK00726 | murG | 6.06e-135 | 2 | 354 | 1 | 356 | undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
| COG0707 | MurG | 1.51e-111 | 3 | 351 | 1 | 349 | UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]. |
| cd03785 | GT28_MurG | 9.46e-109 | 4 | 332 | 1 | 331 | 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. |
| pfam03033 | Glyco_transf_28 | 8.42e-46 | 5 | 143 | 1 | 139 | Glycosyltransferase family 28 N-terminal domain. The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AYH40137.1 | 3.82e-138 | 1 | 356 | 1 | 353 |
| CBK75427.1 | 5.50e-133 | 3 | 349 | 2 | 349 |
| AVQ47989.1 | 2.30e-132 | 3 | 349 | 2 | 349 |
| AVQ53992.1 | 2.30e-132 | 3 | 347 | 2 | 351 |
| AVQ44446.1 | 2.30e-132 | 3 | 349 | 2 | 349 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3S2U_A | 1.64e-41 | 1 | 355 | 1 | 353 | Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1] |
| 1F0K_A | 2.31e-40 | 3 | 354 | 7 | 355 | 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] |
| 7D1I_A | 2.57e-36 | 3 | 346 | 10 | 359 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q97GY4 | 2.21e-132 | 4 | 349 | 5 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=murG PE=3 SV=1 |
| A7GGX9 | 3.50e-130 | 3 | 347 | 2 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=murG PE=3 SV=1 |
| B1IKH3 | 3.50e-130 | 3 | 347 | 2 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Clostridium botulinum (strain Okra / Type B1) OX=498213 GN=murG PE=3 SV=1 |
| C3L230 | 2.00e-129 | 3 | 347 | 2 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Clostridium botulinum (strain 657 / Type Ba4) OX=515621 GN=murG PE=3 SV=1 |
| A7FX11 | 2.84e-129 | 3 | 347 | 2 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 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 |
|---|---|---|---|---|---|
| 1.000059 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |