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CAZyme Information: MGYG000001344_00571

You are here: Home > Sequence: MGYG000001344_00571

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 Acinetobacter radioresistens
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter radioresistens
CAZyme ID MGYG000001344_00571
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
365 39500.22 9.9072
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001344 3137190 Isolate not provided not provided
Gene Location Start: 267550;  End: 268647  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001344_00571.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT28 195 354 6e-51 0.9872611464968153

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK00726 murG 9.02e-164 9 365 1 354
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785 GT28_MurG 2.57e-137 11 361 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 1.35e-128 12 365 3 354
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133 murG 2.01e-124 10 362 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]
pfam03033 Glyco_transf_28 2.51e-44 12 146 1 135
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
QCS13432.1 2.59e-256 1 365 1 365
QMU06607.1 2.59e-256 1 365 1 365
BBL21998.1 2.59e-256 1 365 1 365
AWV87592.1 5.23e-256 1 365 1 365
QJG85032.1 1.44e-214 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
7D1I_A 7.49e-216 1 365 1 365
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]
3S2U_A 2.14e-104 11 360 4 349
Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]
1F0K_A 7.17e-83 10 365 7 353
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A3M9Y1 4.10e-215 1 365 1 365
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377) OX=400667 GN=murG PE=3 SV=2
B7ICE5 8.27e-215 1 365 1 365
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Acinetobacter baumannii (strain AB0057) OX=480119 GN=murG PE=3 SV=1
B0V9F5 8.27e-215 1 365 1 365
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Acinetobacter baumannii (strain AYE) OX=509173 GN=murG PE=3 SV=1
B7GV73 8.27e-215 1 365 1 365
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Acinetobacter baumannii (strain AB307-0294) OX=557600 GN=murG PE=3 SV=1
B2I1J5 2.75e-213 1 365 1 365
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Acinetobacter baumannii (strain ACICU) OX=405416 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
1.000071 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001344_00571.