CAZyme Information: MGYG000001676_00517

Basic Information

• Species: RUG705 sp900759875
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; RUG705; RUG705 sp900759875
• CAZyme ID: MGYG000001676_00517
• 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		40856.09	10.0952

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001676	1153275	MAG	United States	North America

• Gene Location: Start: 126363; End: 127457 Strand: -

Full Sequence      

MRVVISAGGTGGHIYPAIAIINKIKEKEPNSEILYIGTTNRMEKDLIPELGIKYEEINVS
GLKRKITLENFKVLLQFLKAREKCKKIIKEFDPDVVIGAGGYVTGPVIWAGKKLGKKTFI
HEQNSVVGLSNKYLTKYADKIGVSFASTMKYFPKDKVVLTGNPCSQKALDVKKANKEDFG
LTKNKKLVLIVMGSLGSKTVNDKIVTFLDAFKTKDYEVMFVTGNSYYEKVKNLKTPQNVK
IVPFIYEMPSLMKSTDLMITRAGATTMSEILVLGVPAIFIPSPYVTNNHQYKNAMDLANK
NAALILEEKDLTKVNLINLIDKTLANKEEYNNIKNNLKKLGIKDSSERIYELLKGMIMDD
KKFF

Enzyme Prediction     

No EC number prediction in MGYG000001676_00517.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT28	188	344	3.3e-46	0.9808917197452229

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00726	murG	1.31e-147	1	357	2	355	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785	GT28_MurG	6.96e-140	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.
COG0707	MurG	1.43e-117	1	354	1	352	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133	murG	8.50e-116	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]
pfam03033	Glyco_transf_28	1.45e-46	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
AMX80346.1	3.84e-116	1	357	1	362
BCA32964.1	3.84e-116	1	357	1	362
AJA22942.1	3.84e-116	1	357	1	362
QEL82228.1	3.84e-116	1	357	1	362
ANN35394.1	3.84e-116	1	357	1	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D1I_A	1.97e-45	2	328	11	337	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	1.45e-44	2	349	8	346	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	2.42e-40	2	328	4	326	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
Q812W5	1.77e-115	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
A7GRN6	1.77e-115	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
B7GGI2	2.42e-115	1	357	1	362	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
Q636B6	1.01e-114	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
Q6HEQ4	1.01e-114	1	357	1	362	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 1 OS=Bacillus thuringiensis subsp. konkukian (strain 97-27) OX=281309 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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001676_00517.