dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001600_00616

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Basic Information help

Species

Lineage

Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; ;

CAZyme ID

MGYG000001600_00616

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	MGYG000001600_124\|CGC1	40319.07	7.1523

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001600	1449381	MAG	China	Asia

Gene Location

Start: 1674; End: 2801 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001600_00616.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT28	187	351	7.8e-48	0.9936305732484076

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK00726	murG	7.95e-130	1	352	2	344	undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785	GT28_MurG	2.29e-124	2	354	1	346	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	3.86e-103	1	354	1	346	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133	murG	3.14e-93	1	352	1	341	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	2.34e-42	3	140	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV56058.1	1.67e-167	1	353	1	353
QOS67217.1	2.37e-167	1	353	1	353
BAK44146.1	8.13e-166	1	353	1	353
ANE22900.1	1.34e-163	1	354	1	354
VEG99762.1	6.38e-160	1	352	1	352

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3S2U_A	8.12e-54	2	351	4	343	Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]
7D1I_A	9.99e-51	2	327	11	330	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]
1F0K_A	3.72e-44	2	312	8	305	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]
4WYI_A	3.24e-06	152	285	176	312	Thecrystal structure of Arabidopsis thaliana galactolipid synthase, MGD1 (apo-form) [Arabidopsis thaliana],4X1T_A The crystal structure of Arabidopsis thaliana galactolipid synthase MGD1 in complex with UDP [Arabidopsis thaliana]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A3DE27	1.55e-73	1	314	1	314	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
B8CWJ6	4.60e-73	1	330	1	335	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562) OX=373903 GN=murG PE=3 SV=1
Q24TE6	3.42e-72	1	354	1	358	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Desulfitobacterium hafniense (strain Y51) OX=138119 GN=murG PE=3 SV=1
B8FT56	1.91e-71	1	354	1	358	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Desulfitobacterium hafniense (strain DSM 10664 / DCB-2) OX=272564 GN=murG PE=3 SV=1
B1I4C4	2.14e-71	1	317	1	322	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Desulforudis audaxviator (strain MP104C) OX=477974 GN=murG PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000001600_00616.