CAZyme Information: MGYG000001752_00549

Basic Information

• Species: CAG-1000 sp000436975
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-1000; CAG-1000 sp000436975
• CAZyme ID: MGYG000001752_00549
• 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
368	MGYG000001752_3|CGC1	41480.54	9.808

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001752	1197670	MAG	Sweden	Europe

• Gene Location: Start: 3388; End: 4494 Strand: -

Full Sequence      

MKFILTAGGTGGHIYPALSVLDEIKKDKKNEYLYIGTEDRMESELIPGMGIPFVGLEIYG
LSKTNIIRNIKNIGCIVSSYRKCLKIIDEFKPDAVIAFGGYVTLPVCLAAKKRKVKVFLH
EQNMLPGKTNIFLSKYADAVFTSFKDGMRKLKCKNIIYTGNPVSQRAIECKKYNKTNLGF
TKEKKLIVIVMGSLGSTSVNERILDFLRTFEREDTEILFITGKKSFNDLNNNLIVPKSTK
IVPFFDNLPTIMKSSDLIISRAGASTIAEIMATKTPSILIPSPYVANNHQYYNALDLVNK
KISIMLEEKDLNTESLTNAIDEMFDEETFKEVRNNLREIKDISSSTIILDKVKEILGNKN
EKKSKKKI

Enzyme Prediction     

No EC number prediction in MGYG000001752_00549.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT28	187	339	3.8e-40	0.9554140127388535

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00726	murG	1.42e-126	1	357	2	356	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785	GT28_MurG	8.83e-124	2	350	1	349	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	1.94e-103	1	355	1	354	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133	murG	4.14e-99	1	352	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	4.19e-41	3	142	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBK62151.1	2.63e-86	1	350	1	350
BBK22068.1	2.63e-86	1	350	1	350
ANU70205.1	6.99e-81	1	330	1	329
QJA03401.1	6.99e-81	1	330	1	329
ASU17375.1	6.99e-81	1	330	1	329

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D1I_A	4.01e-35	4	355	13	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]
1F0K_A	1.44e-32	2	320	8	319	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	3.90e-32	4	355	6	354	Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O07670	1.37e-76	1	323	1	324	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Enterococcus hirae OX=1354 GN=murG PE=3 SV=1
Q65JY0	1.63e-76	1	333	1	339	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=murG PE=3 SV=1
B7GGI2	8.37e-76	1	321	1	326	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Anoxybacillus flavithermus (strain DSM 21510 / WK1) OX=491915 GN=murG PE=3 SV=1
Q9K9T0	2.35e-75	1	323	1	328	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=murG PE=3 SV=1
Q1WTA0	7.02e-75	1	326	1	332	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Ligilactobacillus salivarius (strain UCC118) OX=362948 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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001752_00549.