CAZyme Information: MGYG000003369_00063

Basic Information

• Species: Anaerococcus sp900258475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus; Anaerococcus sp900258475
• CAZyme ID: MGYG000003369_00063
• 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
361	MGYG000003369_1|CGC2	40123.24	9.2915

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003369	1844507	MAG	United States	North America

• Gene Location: Start: 71266; End: 72351 Strand: +

Full Sequence      

MKRAIITGGGTGGHIYPAIAIGDKIKEENPGVEILYVGIKGGPEERIAKKNGYKFHSIEA
MGIPRKINKRLFKSLLANIKGFGQAKKIIKDFKPELVVGTGGYVCAPILYQAARAHIPSI
VHESNSYPGMASKFLSQRVDKVLISYEEAKKHFKYQKNIVVTGNPVRNNFNLTYTEEDLK
SLGIDEDKPIVFSFGGSNGSYALNQAVLELSKKLDGKYYLLHQTGNRYYDDFVKKASPSK
YLKVFEYIDNIDLFYGLADLIIASSGAMSLAEISSVGKASILIPKAYTTENHQEYNARTY
MDHGASLMILEKDLKADLLNDSILSIIKDKDTMQKMGEEAYKLADMSATDKIYSEITKLI
D

Enzyme Prediction     

No EC number prediction in MGYG000003369_00063.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT28	191	345	1.8e-41	0.9681528662420382

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03785	GT28_MurG	3.74e-121	14	355	12	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.
PRK00726	murG	1.39e-120	14	360	14	355	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
TIGR01133	murG	1.34e-93	14	356	13	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	4.65e-93	14	360	13	355	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
pfam03033	Glyco_transf_28	6.01e-37	14	144	11	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
ACV29227.1	2.48e-181	3	360	2	359
QQN56060.1	1.30e-166	3	360	2	359
QQB61390.1	3.72e-166	3	360	2	359
AXU11211.1	1.52e-113	3	354	2	360
VEH95021.1	3.83e-113	3	354	9	367

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1F0K_A	3.17e-39	2	359	7	353	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	1.70e-38	2	359	10	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]
3S2U_A	6.61e-36	3	349	4	344	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
B0S0Z5	1.41e-107	5	361	4	365	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508) OX=334413 GN=murG PE=3 SV=1
A8MH36	1.25e-99	3	361	2	364	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Alkaliphilus oremlandii (strain OhILAs) OX=350688 GN=murG PE=3 SV=1
A3DE27	4.05e-96	3	360	2	363	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
Q182Y6	3.94e-95	1	359	1	365	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Clostridioides difficile (strain 630) OX=272563 GN=murG PE=3 SV=1
B0K3H0	5.74e-92	3	359	2	363	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Thermoanaerobacter sp. (strain X514) OX=399726 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
1.000037	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003369_00063.