CAZyme Information: MGYG000002513_01914

Basic Information

• Species: Morganella morganii_A
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Morganella; Morganella morganii_A
• CAZyme ID: MGYG000002513_01914
• 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
357	MGYG000002513_155|CGC1	38133.9	8.6785

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002513	3981937	Isolate	United States	North America

• Gene Location: Start: 2237; End: 3310 Strand: +

Full Sequence      

MSNKAPRLMVMAGGSGGHVFPGLAVAHYLQSQGWEIRWLGTRDRMEAQLVPKHGIDIDFI
EITGLRGKGVKALLTAPFRIAKAIKQAKKIMRDYQPDAVLGMGGFVSGPGGVAAWRCGIP
VILHEQNGVAGLTNGWLSKIATTVLQGFPGAFPQAPVVGNPVREDILNLPSPAERFAGRE
GPVRILVIGGSQGARVLNQTLPEVAGIMGDAVCIRHQAGKGSAESTQELYNAQGASDSVT
VTEFIDDMVEAYTWADVVICRSGALTVSEIAVVGLGAIFVPFQHKDRQQYWNALPLEQAG
AAVITEQPSFNAQAVAEQLREWDRPRLLTMAEKARSVAITDATKRVADAIIAAAKKN

Enzyme Prediction     

No EC number prediction in MGYG000002513_01914.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT28	185	342	7.9e-46	0.9872611464968153

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00726	murG	2.11e-173	6	346	2	347	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
TIGR01133	murG	1.90e-144	7	346	2	344	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]
cd03785	GT28_MurG	2.47e-144	7	346	1	347	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	8.84e-142	7	346	2	347	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
pfam03033	Glyco_transf_28	1.32e-52	8	146	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
QXO64543.1	8.38e-258	1	357	1	357
QXO71991.1	8.38e-258	1	357	1	357
QXO75810.1	1.69e-257	1	357	1	357
QXO79642.1	1.69e-257	1	357	1	357
QXO56850.1	1.69e-257	1	357	1	357

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1F0K_A	4.84e-177	1	350	2	350	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	3.96e-86	3	350	7	362	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	8.94e-85	8	355	5	356	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
Q7N147	3.52e-186	1	356	1	355	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) OX=243265 GN=murG PE=3 SV=1
A1JJJ3	2.88e-185	1	355	1	355	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) OX=393305 GN=murG PE=3 SV=1
B4F111	2.82e-184	1	356	1	360	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Proteus mirabilis (strain HI4320) OX=529507 GN=murG PE=3 SV=1
A8G9S7	1.07e-182	1	355	1	354	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Serratia proteamaculans (strain 568) OX=399741 GN=murG PE=3 SV=1
A7FM66	5.16e-179	1	355	1	354	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Yersinia pseudotuberculosis serotype O:1b (strain IP 31758) OX=349747 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
1.000038	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002513_01914.