CAZyme Information: MGYG000001273_00886

Basic Information

• Species: Pauljensenia sp902373435
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Pauljensenia; Pauljensenia sp902373435
• CAZyme ID: MGYG000001273_00886
• 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
374	MGYG000001273_36|CGC1	38355.95	6.694

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001273	2113963	MAG	Italy	Europe

• Gene Location: Start: 8932; End: 10056 Strand: +

Full Sequence      

MVKVVMAGGGTAGHVNPLLATAAQLRASGAEVVVLVTKAGLEADLVPAAGFPLVEMPRVP
LPRRPSLAFFTLPGRFADAVKRCTQALQGADVLVGFGGYVSTPAYIAAKRAGVPIVIHEQ
NARPGLANKVGARNAKVVALTFPSSPLKARNGDTTVTGLPLRAAIAELASHRADAQGAAQ
ARREAAERLGVDPDAPTLLVTGGSLGALHVNESMTGAADALPEGAQVVHLTGRGKDEPVR
AAVEAAGLSDRWHVIDYLTTMEDALAVADLVVCRSGAGTVAEMEALGLPCIYVPLPIGNG
EQRLNAADHVAAGGAQLIDDKDFTADCVRRNVFPLLGSTRLADMAAASQSLGRAGAARAL
ADLALEQVKEAGHE

Enzyme Prediction     

No EC number prediction in MGYG000001273_00886.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT28	197	354	3.1e-44	0.9808917197452229

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00726	murG	2.26e-116	1	350	1	337	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785	GT28_MurG	2.91e-101	3	350	1	337	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	1.19e-85	3	350	2	337	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133	murG	4.90e-84	3	350	2	334	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	1.60e-36	4	139	1	138	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
QCT35695.1	4.39e-248	1	374	1	374
QGS10808.1	5.81e-237	1	374	1	374
QQC44616.1	3.15e-218	1	374	1	374
AKU64718.1	3.15e-218	1	374	1	374
AOS47979.1	1.66e-188	6	366	1	361

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1F0K_A	3.07e-39	3	328	8	315	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	1.69e-36	4	363	12	361	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	2.33e-33	3	373	4	360	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
B7GQ78	6.02e-94	4	361	8	382	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) OX=391904 GN=murG PE=3 SV=1
Q8CY50	6.02e-94	4	361	8	382	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bifidobacterium longum (strain NCC 2705) OX=206672 GN=murG PE=3 SV=1
B3DQN1	6.02e-94	4	361	8	382	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bifidobacterium longum (strain DJO10A) OX=205913 GN=murG PE=3 SV=1
A0JV94	1.05e-93	3	370	7	366	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Arthrobacter sp. (strain FB24) OX=290399 GN=murG PE=3 SV=1
A1A2E9	1.36e-92	4	336	7	355	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 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
0.999913	0.000138	0.000008	0.000000	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001273_00886.