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CAZyme Information: MGYG000004520_01223

You are here: Home > Sequence: MGYG000004520_01223

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 Ruminococcus_E bromii_A
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E bromii_A
CAZyme ID MGYG000004520_01223
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
372 MGYG000004520_14|CGC1 40219.54 9.9227
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004520 2155170 MAG Israel Asia
Gene Location Start: 41593;  End: 42711  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004520_01223.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT28 192 356 9.3e-52 0.9808917197452229

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK00726 murG 2.64e-148 1 370 2 356
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785 GT28_MurG 1.94e-146 2 364 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 8.86e-122 1 368 1 354
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133 murG 1.22e-105 1 365 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]
pfam04101 Glyco_tran_28_C 3.42e-43 191 361 1 166
Glycosyltransferase family 28 C-terminal domain. The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCT06982.1 7.22e-188 1 370 1 371
QAT50143.1 1.11e-164 1 369 1 370
QEY33586.1 1.42e-164 1 370 1 371
CAB1239505.1 1.83e-163 1 369 1 370
QKO29751.1 6.05e-162 1 369 1 370

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1F0K_A 2.44e-55 2 368 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 9.84e-50 2 368 4 354
Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]
7D1I_A 1.05e-48 2 368 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A3DE27 9.02e-114 1 369 1 363
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
Q812W5 1.11e-97 1 369 1 362
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 1 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=murG1 PE=3 SV=1
A7GRN6 1.57e-97 1 369 1 362
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98) OX=315749 GN=murG PE=3 SV=1
B0K3H0 4.44e-97 1 368 1 363
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=murG PE=3 SV=1
A0RHT1 4.44e-97 1 369 1 362
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 2 OS=Bacillus thuringiensis (strain Al Hakam) OX=412694 GN=murG2 PE=3 SV=2

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
1.000062 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004520_01223.