CAZyme Information: MGYG000004802_00242

Basic Information

• Species: UMGS1384 sp900551265
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Butyricicoccaceae; UMGS1384; UMGS1384 sp900551265
• CAZyme ID: MGYG000004802_00242
• 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
375	MGYG000004802_7|CGC1	40962.35	8.4626

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004802	2084927	MAG	Spain	Europe

• Gene Location: Start: 11693; End: 12820 Strand: -

Full Sequence      

MRVLIGTGGTGGHINPAIAIAKNIMTRSPDSEVLFCGASGGLEEKLVVREGFPLETFDIK
GFRRSLKPAGFAYNFKILGKVRRAIADARTVIERFHPDIAIGCGGYASFPIVYAAQSKGV
PTALLEVNALPGITTKVLARRADTVMISFEESRALIKSDRIVLTGSPVREDILFAKKDEA
RRELGLDARPLIVSVWGSLGAERMNHVMTDFVALEAKEDRHNLIHAIGSYGYTWVRNEIR
EKGVDLSKHPNIDIRDYIYDAARVYAAADVVLCRAGAATLGEMAMMGKPVVIVPSPNVAE
NHQEKNARAIEREGGAVVILERDCTAELLYDTVCKLLADPARLQQMSHNISKFAVPDAMD
KIYASICAAVRQSRT

Enzyme Prediction     

No EC number prediction in MGYG000004802_00242.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT28	195	358	4.9e-43	0.9681528662420382

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00726	murG	4.29e-108	13	371	14	356	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785	GT28_MurG	2.47e-106	13	364	12	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	8.04e-87	13	372	13	357	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133	murG	6.16e-79	1	366	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]
pfam04101	Glyco_tran_28_C	2.45e-34	197	362	7	166	Glycosyltransferase family 28 C-terminal domain. The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUO37394.1	1.71e-118	2	366	7	373
QCI58785.1	2.24e-116	2	366	7	373
BAK98610.1	3.40e-115	2	366	7	372
QIA29973.1	1.88e-114	1	366	1	366
QQR06670.1	4.93e-112	1	366	1	366

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3S2U_A	3.97e-43	2	358	4	343	Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]
1F0K_A	3.07e-40	2	371	8	355	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	2.35e-38	2	362	11	358	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
B8I6H3	2.03e-93	1	363	1	357	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=murG PE=3 SV=1
A3DE27	2.15e-91	1	366	1	359	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=murG PE=3 SV=1
B0K3H0	7.37e-91	1	366	1	360	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Thermoanaerobacter sp. (strain X514) OX=399726 GN=murG PE=3 SV=1
B0K8K7	7.37e-91	1	366	1	360	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=murG PE=3 SV=1
Q8R9G6	3.33e-89	1	363	1	357	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) OX=273068 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
1.000065	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004802_00242.