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CAZyme Information: MGYG000000708_00733
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Succinivibrionaceae; Succinivibrio; | |||||||||||
| CAZyme ID | MGYG000000708_00733 | |||||||||||
| 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: 1268; End: 2329 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT28 | 180 | 336 | 4.8e-53 | 0.9681528662420382 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK00726 | murG | 2.68e-162 | 1 | 350 | 2 | 354 | undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
| cd03785 | GT28_MurG | 1.47e-147 | 2 | 339 | 1 | 343 | 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. |
| TIGR01133 | murG | 1.00e-127 | 1 | 350 | 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] |
| COG0707 | MurG | 6.64e-125 | 1 | 351 | 1 | 355 | UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]. |
| pfam03033 | Glyco_transf_28 | 4.42e-45 | 3 | 140 | 1 | 138 | 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 |
|---|---|---|---|---|---|
| QVK24786.1 | 2.77e-130 | 2 | 350 | 7 | 358 |
| QUM87560.1 | 4.93e-126 | 2 | 350 | 4 | 351 |
| QUM83258.1 | 4.93e-126 | 2 | 350 | 4 | 351 |
| QUN06137.1 | 4.53e-125 | 2 | 350 | 9 | 360 |
| QFI39791.1 | 6.28e-125 | 2 | 339 | 4 | 340 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7D1I_A | 3.19e-95 | 2 | 350 | 11 | 365 | 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] |
| 1F0K_A | 1.99e-93 | 2 | 350 | 8 | 353 | 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] |
| 3S2U_A | 1.87e-91 | 2 | 335 | 4 | 339 | Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8CX35 | 1.20e-117 | 2 | 346 | 7 | 354 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Shewanella oneidensis (strain MR-1) OX=211586 GN=murG PE=3 SV=1 |
| A0L1P2 | 3.41e-117 | 2 | 346 | 7 | 354 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Shewanella sp. (strain ANA-3) OX=94122 GN=murG PE=3 SV=1 |
| Q0HZR6 | 3.41e-117 | 2 | 346 | 7 | 354 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Shewanella sp. (strain MR-7) OX=60481 GN=murG PE=3 SV=1 |
| Q0HE83 | 1.38e-116 | 2 | 346 | 7 | 354 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Shewanella sp. (strain MR-4) OX=60480 GN=murG PE=3 SV=1 |
| A6WID1 | 1.95e-116 | 2 | 350 | 7 | 358 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Shewanella baltica (strain OS185) OX=402882 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 |
|---|---|---|---|---|---|
| 1.000070 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |