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CAZyme Information: MGYG000002074_00468

You are here: Home > Sequence: MGYG000002074_00468

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 QAMH01 sp900556425
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; QAMH01; QAMH01; QAMH01 sp900556425
CAZyme ID MGYG000002074_00468
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
370 MGYG000002074_3|CGC1 39552.22 5.9209
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002074 2149037 MAG Netherlands Europe
Gene Location Start: 49874;  End: 50986  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002074_00468.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT28 189 351 1.7e-48 0.9808917197452229

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK00726 murG 4.75e-126 1 366 2 357
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785 GT28_MurG 1.08e-120 3 359 2 350
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 1.40e-106 1 366 1 357
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133 murG 3.07e-100 1 358 1 346
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 3.70e-43 4 362 5 351
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QTU84759.1 2.15e-128 1 365 1 364
VEG99762.1 2.56e-121 1 365 1 364
ACV21932.1 2.56e-121 1 365 1 364
AJC12321.1 3.10e-119 1 364 1 363
ANE22900.1 5.13e-118 1 360 1 359

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3S2U_A 3.38e-50 4 366 6 357
Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]
1F0K_A 1.79e-49 4 365 10 355
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 3.36e-44 2 362 11 364
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]
2IYA_A 8.23e-09 12 361 24 417
Thecrystal structure of macrolide glycosyltransferases: A blueprint for antibiotic engineering [Streptomyces antibioticus],2IYA_B The crystal structure of macrolide glycosyltransferases: A blueprint for antibiotic engineering [Streptomyces antibioticus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B8CWJ6 9.92e-74 1 367 1 371
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
B8FT56 1.12e-68 1 363 1 363
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Desulfitobacterium hafniense (strain DSM 10664 / DCB-2) OX=272564 GN=murG PE=3 SV=1
Q24TE6 1.12e-68 1 359 1 362
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Desulfitobacterium hafniense (strain Y51) OX=138119 GN=murG PE=3 SV=1
A3DE27 1.52e-65 1 361 1 360
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
B1MXW0 3.01e-65 1 362 1 362
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Leuconostoc citreum (strain KM20) OX=349519 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
1.000052 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002074_00468.