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CAZyme Information: MGYG000000304_00369

You are here: Home > Sequence: MGYG000000304_00369

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 CAG-1427 sp900542525
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; CAG-1427; CAG-1427 sp900542525
CAZyme ID MGYG000000304_00369
CAZy Family GT28
CAZyme Description UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
366 MGYG000000304_3|CGC1 38945.49 4.948
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000304 1613120 MAG Sweden Europe
Gene Location Start: 26821;  End: 27921  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000304_00369.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT28 187 351 5.6e-49 0.9936305732484076

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK00726 murG 6.49e-122 1 364 2 356
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785 GT28_MurG 7.37e-113 2 358 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 7.12e-95 1 365 1 357
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133 murG 4.94e-88 1 359 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 6.22e-43 3 329 4 322
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QOS67217.1 5.88e-168 1 366 1 366
ANE22900.1 2.49e-166 1 364 1 364
QTU84759.1 5.97e-166 1 365 1 365
ACV56058.1 1.12e-165 1 366 1 366
BAK44146.1 4.45e-163 1 362 1 362

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7D1I_A 7.33e-52 2 326 11 334
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 8.39e-50 2 364 4 356
Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]
1F0K_A 8.83e-42 3 323 9 316
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]
4WYI_A 9.93e-07 152 307 176 331
Thecrystal structure of Arabidopsis thaliana galactolipid synthase, MGD1 (apo-form) [Arabidopsis thaliana],4X1T_A The crystal structure of Arabidopsis thaliana galactolipid synthase MGD1 in complex with UDP [Arabidopsis thaliana]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B8CWJ6 8.87e-77 1 330 1 335
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562) OX=373903 GN=murG PE=3 SV=1
Q8Y5M2 6.12e-72 1 364 1 363
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) OX=169963 GN=murG PE=3 SV=1
Q9K9T0 8.63e-72 1 364 1 363
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=murG PE=3 SV=1
Q71XX8 3.42e-71 1 364 1 363
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Listeria monocytogenes serotype 4b (strain F2365) OX=265669 GN=murG PE=3 SV=1
C1KWY8 3.42e-71 1 364 1 363
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Listeria monocytogenes serotype 4b (strain CLIP80459) OX=568819 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
1.000064 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000304_00369.