CAZyme Information: MGYG000003724_00505

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus
• CAZyme ID: MGYG000003724_00505
• 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
364	MGYG000003724_24|CGC1	40198.35	9.346

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003724	1472545	MAG	Canada	North America

• Gene Location: Start: 2515; End: 3609 Strand: -

Full Sequence      

MRVIMSGGGTGGHIYPAIAIAQKLQANIENCEILYVGIKGGPEEAIAKKYGYDFKPIDGM
GLPRKINKRFFKSLSKNMKGFKAARKIVKEFKPDIAIGTGGYVCGPIIYKASKANVPTII
HESNSYPGVTSKFLSKRVDYLCISYPQAKRHLKYKDNIVVTGNPVRTNFKETFTDEDLAK
LGIKKDRPVVFSFGGSNGSYALNKAVIELSKILKDEFYLLHQTGRRNYDKFNEEVTDNPY
IKAFSYIDNIDLFYAVSDLVIASSGAMSLAEISAVKKPSILIPKAYTTENHQQYNAQTYV
DNGAALMILEKNLDGKILYDDIVSIIDDKNKLEAMGKAAGSLADEDASDKILDLVLELVG
KDAK

Enzyme Prediction     

No EC number prediction in MGYG000003724_00505.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT28	190	347	1.8e-44	0.9872611464968153

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00726	murG	3.13e-135	1	361	2	357	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785	GT28_MurG	9.60e-133	2	354	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	1.34e-103	1	361	1	357	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133	murG	3.27e-100	1	355	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	2.17e-43	3	139	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV29227.1	7.16e-177	1	359	1	359
QQB61390.1	3.14e-175	1	360	1	360
QQN56060.1	6.33e-175	1	360	1	360
VEH95021.1	1.96e-111	1	343	8	357
AXU11211.1	3.14e-111	1	343	1	350

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D1I_A	1.20e-41	2	358	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]
3S2U_A	1.28e-39	2	358	4	354	Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]
1F0K_A	4.74e-39	2	355	8	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B0S0Z5	7.20e-106	1	364	1	369	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508) OX=334413 GN=murG PE=3 SV=1
A3DE27	7.91e-97	1	359	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
A8MH36	9.28e-95	1	351	1	355	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Alkaliphilus oremlandii (strain OhILAs) OX=350688 GN=murG PE=3 SV=1
Q182Y6	1.58e-92	1	364	2	371	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Clostridioides difficile (strain 630) OX=272563 GN=murG PE=3 SV=1
Q8R9G6	1.59e-92	1	355	1	360	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) OX=273068 GN=murG PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003724_00505.