CAZyme Information: MGYG000000244_00565

Basic Information

• Species: Catenibacterium sp000437715
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Catenibacterium; Catenibacterium sp000437715
• CAZyme ID: MGYG000000244_00565
• 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
362	MGYG000000244_6|CGC1	39776.37	8.043

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000244	2463343	Isolate	China	Asia

• Gene Location: Start: 48129; End: 49217 Strand: +

Full Sequence      

MKIIVSAGGTGGHIYPALALVDYIKKCDPDTEFLFVGTTDRLESQIVPQMGLAYRGLHVK
GLVGNPLQKAKNALIFLKSLKSSKKILKEFNPDIVIGFGGYPSASIVLAASQKGYKTMIH
EQNSIIGLTNKILIKRVDEIVCCYEKALKAFPQDKTKLLGNPRASVVSEGVLKDVHDLYN
IAPDRKVMVIVMGSLGSATVNAVMKDALHKMDHKDYDVLYVTGKTYYEKMKEELKDLSDS
IHVLPYIDDMPSVLHSCDLAVSRAGATTLAEMTALGTASIIIPSPYVVANHQEYNARELV
AKGAAHLILEKDLNADAFVEVVDQYMNNEEMRKELSKKALALGKPYACEDIYKEILKLTG
GR

Enzyme Prediction     

No EC number prediction in MGYG000000244_00565.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT28	189	345	3.8e-46	0.9681528662420382

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00726	murG	1.31e-131	1	361	2	357	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785	GT28_MurG	3.02e-129	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	7.69e-104	1	358	1	354	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133	murG	1.07e-91	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	2.24e-39	3	140	1	137	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
BBH27515.1	2.75e-185	1	358	1	358
QUN13167.1	5.81e-180	1	357	1	357
BCL58428.1	3.22e-157	1	360	1	357
QMW75020.1	4.71e-152	1	358	1	358
QPS11709.1	4.71e-152	1	358	1	358

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3S2U_A	7.18e-45	2	361	4	357	Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]
1F0K_A	8.99e-38	2	359	8	354	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	1.78e-37	3	358	12	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q812W5	1.07e-100	1	359	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
Q81JG5	4.28e-100	1	359	1	362	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 1 OS=Bacillus anthracis OX=1392 GN=murG1 PE=3 SV=1
Q6HEQ4	4.28e-100	1	359	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
Q636B6	4.28e-100	1	359	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
A0RHT1	4.28e-100	1	359	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000052	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000244_00565.