CAZyme Information: MGYG000003672_00297

Basic Information

• Species: CAG-594 sp900772415
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-594; CAG-594 sp900772415
• CAZyme ID: MGYG000003672_00297
• 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	MGYG000003672_31|CGC1	40931.08	9.9841

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003672	1172535	MAG	Peru	South America

• Gene Location: Start: 55253; End: 56350 Strand: +

Full Sequence      

MRVIISAGGTGGHIYPALAIANKIKEKDKSAEILYIGTKNRMEKDIVPSYGYKFIGISVE
GLKRSLSPRNIKSVILFINSIRKCKNIIKKFKPDVVIGVGGYVSAPTVYAAYKLGIKCCI
HEQNSCFGMTNKFLSKYADKVFVSFKSLEEKMNDKKIIYTGNPCSENAINIVPALKSDYG
LSDTKKLVLIVMGSLGSKTINNKMKTMLTLFNNKDYEVLFVTGKNYYDEYKNLNYTKNIK
IVPYIDNMVSLLKKVDCLVSRAGATTLSEISSLNVISILIPSPYVTENHQYKNAMDLVSK
EAALILEEKDLKGDNLLRMVEKVLNNKVYANKIKKNLKEFEVKNSASMIYDEIVKLVGIK
NERSN

Enzyme Prediction     

No EC number prediction in MGYG000003672_00297.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT28	188	342	1.3e-42	0.9681528662420382

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00726	murG	1.63e-139	1	358	2	356	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785	GT28_MurG	2.71e-136	2	352	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.
TIGR01133	murG	2.49e-110	1	353	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	1.26e-108	1	357	1	355	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
pfam03033	Glyco_transf_28	1.57e-49	3	143	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
QEU38216.1	4.80e-104	1	351	1	356
QHB51714.1	2.73e-103	1	351	1	356
QIR08996.1	5.48e-103	1	351	1	356
AEN99411.1	1.83e-102	1	349	1	355
QFX94215.1	1.83e-102	1	349	1	355

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1F0K_A	4.42e-42	2	314	8	313	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	1.31e-39	2	325	11	335	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	7.24e-34	2	324	4	322	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
Q1WTA0	2.79e-99	1	349	1	355	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Ligilactobacillus salivarius (strain UCC118) OX=362948 GN=murG PE=3 SV=1
A7GRN6	1.53e-98	1	357	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
Q812W5	4.35e-98	1	357	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
Q8Y5M2	4.79e-97	1	357	1	362	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) OX=169963 GN=murG PE=3 SV=1
Q636B6	4.94e-97	1	357	1	362	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 1 OS=Bacillus cereus (strain ZK / E33L) OX=288681 GN=murG1 PE=3 SV=2

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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003672_00297.