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CAZyme Information: MGYG000002368_02299

You are here: Home > Sequence: MGYG000002368_02299

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 Vibrio metoecus
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio metoecus
CAZyme ID MGYG000002368_02299
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
353 MGYG000002368_20|CGC3 37822.81 8.4805
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002368 3946363 Isolate United States North America
Gene Location Start: 82268;  End: 83329  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002368_02299.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT28 184 339 2.2e-47 0.9808917197452229

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK00726 murG 9.83e-172 4 353 1 356
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
TIGR01133 murG 3.14e-157 5 348 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 4.07e-144 5 351 1 354
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
cd03785 GT28_MurG 1.81e-139 6 345 1 348
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.
pfam03033 Glyco_transf_28 1.78e-53 7 145 1 139
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
SYZ80576.1 2.82e-238 1 353 1 353
QGF32498.1 5.68e-238 1 353 1 353
QUX98691.1 5.68e-238 1 353 1 353
ABQ21490.1 5.90e-238 1 353 2 354
ACP10505.1 5.90e-238 1 353 2 354

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1F0K_A 5.60e-156 3 348 5 350
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 1.17e-92 2 340 7 354
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 4.67e-92 7 351 5 354
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
A5F5M9 1.18e-238 1 353 2 354
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) OX=345073 GN=murG PE=3 SV=1
C3LQU6 1.61e-236 1 353 2 354
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Vibrio cholerae serotype O1 (strain M66-2) OX=579112 GN=murG PE=3 SV=1
Q9KPG7 1.61e-236 1 353 2 354
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=murG PE=3 SV=1
Q87SG4 4.88e-206 1 353 1 353
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) OX=223926 GN=murG PE=3 SV=1
A7MXR6 1.33e-203 1 353 1 353
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Vibrio campbellii (strain ATCC BAA-1116 / BB120) OX=1224742 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
1.000076 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002368_02299.