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CAZyme Information: MGYG000000486_00958
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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 | Phascolarctobacterium_A sp900770955 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_C; Negativicutes; Acidaminococcales; Acidaminococcaceae; Phascolarctobacterium_A; Phascolarctobacterium_A sp900770955 | |||||||||||
| CAZyme ID | MGYG000000486_00958 | |||||||||||
| 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: 110902; End: 112005 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT28 | 189 | 353 | 7.6e-49 | 0.9936305732484076 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK00726 | murG | 2.57e-133 | 1 | 367 | 2 | 357 | undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
| cd03785 | GT28_MurG | 1.60e-132 | 2 | 360 | 1 | 350 | 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. |
| COG0707 | MurG | 5.50e-108 | 1 | 367 | 1 | 357 | UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]. |
| TIGR01133 | murG | 9.43e-98 | 1 | 361 | 1 | 348 | 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] |
| PRK12446 | PRK12446 | 5.06e-45 | 2 | 340 | 3 | 331 | undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QTV77435.1 | 2.83e-261 | 1 | 366 | 1 | 366 |
| BBG64397.1 | 1.27e-195 | 1 | 367 | 1 | 367 |
| QNP76910.1 | 1.27e-195 | 1 | 367 | 1 | 367 |
| ADB47663.1 | 7.19e-165 | 1 | 367 | 1 | 367 |
| AEQ22746.1 | 7.53e-158 | 1 | 365 | 1 | 365 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3S2U_A | 1.29e-53 | 2 | 357 | 4 | 347 | Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1] |
| 1F0K_A | 5.70e-45 | 2 | 360 | 8 | 349 | 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 | 1.14e-44 | 3 | 355 | 12 | 356 | 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 |
|---|---|---|---|---|---|---|
| A3DE27 | 4.06e-116 | 1 | 357 | 1 | 355 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=murG PE=3 SV=1 |
| Q812W5 | 4.88e-116 | 1 | 354 | 1 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 1 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=murG1 PE=3 SV=1 |
| A0RHT1 | 4.88e-116 | 1 | 354 | 1 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 2 OS=Bacillus thuringiensis (strain Al Hakam) OX=412694 GN=murG2 PE=3 SV=2 |
| Q6HEQ4 | 4.88e-116 | 1 | 354 | 1 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 1 OS=Bacillus thuringiensis subsp. konkukian (strain 97-27) OX=281309 GN=murG1 PE=3 SV=2 |
| Q636B6 | 4.88e-116 | 1 | 354 | 1 | 351 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 1 OS=Bacillus cereus (strain ZK / E33L) OX=288681 GN=murG1 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 |
|---|---|---|---|---|---|
| 1.000071 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |