CAZyme Information: MGYG000002385_03556

Basic Information

• Species: Leminorella richardii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Leminorella; Leminorella richardii
• CAZyme ID: MGYG000002385_03556
• CAZy Family: GT0
• CAZyme Description: UDP-N-acetylglucosamine 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
361	MGYG000002385_1|CGC24	40843.79	6.4492

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002385	3976274	Isolate	not provided	not provided

• Gene Location: Start: 3828093; End: 3829178 Strand: -

Full Sequence      

MAPLVHALANDKDFESKVCVTAQHREMLDQVLKLFDIKPDYDLDIMRPGQGLTEITCRIL
EGLKPVLESFKPDVVLVHGDTTTTLATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEEGNR
KLTGHLAMYHFSPTETSKQNLLREAIPDSRIFVTGNTVIDALFWVRDRIHSDTTLREEME
RRYPFLHQNKKIILVTGHRRESFGDGFERICSALAEIARSHPDVQVVYPVHLNPNVREPV
KRILSHIDNVTLIEPQDYLPFVYLMDHAYLILTDSGGIQEEAPSLGKPVLVMRNTTERPE
AVSAGTVRLVGTNIALILEEVSRLLKDENEYHIMSRAHNPYGDGKACQRILDALKNNQVK
L

Enzyme Prediction     

No EC number prediction in MGYG000002385_03556.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0381	WecB	0.0	1	357	19	371	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236	wecB	0.0	1	357	16	364	UDP-N-acetylglucosamine 2-epimerase. This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine. In E. coli, this is the first step in the pathway of enterobacterial common antigen biosynthesis.Members of this orthology group have many gene symbols, often reflecting the overall activity of the pathway and/or operon that includes it. Symbols include epsC (exopolysaccharide C) in Burkholderia solanacerum, cap8P (type 8 capsule P) in Staphylococcus aureus, and nfrC in an older designation based on the effects of deletion on phage N4 adsorption. Epimerase activity was also demonstrated in a bifunctional rat enzyme, for which the N-terminal domain appears to be orthologous. The set of proteins found above the suggested cutoff includes E. coli WecB in one of two deeply branched clusters and the rat UDP-N-acetylglucosamine 2-epimerase domain in the other. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
pfam02350	Epimerase_2	2.11e-153	6	355	1	336	UDP-N-acetylglucosamine 2-epimerase. This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional, in these instances Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of rat Gne is the kinase domain.
cd03786	GTB_UDP-GlcNAc_2-Epimerase	3.47e-152	1	355	15	365	UDP-N-acetylglucosamine 2-epimerase and similar proteins. Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family 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.
cd03801	GT4_PimA-like	1.83e-05	58	337	69	343	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found mainly in certain bacteria and archaea.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQN33861.1	1.07e-206	1	359	16	374
QUT15423.1	2.17e-206	1	359	16	374
QLK59446.1	4.37e-206	1	359	16	374
AZP48621.1	6.20e-206	1	359	16	374
AZP44285.1	6.20e-206	1	359	16	374

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1F6D_A	2.49e-211	2	361	17	376	TheStructure Of Udp-N-Acetylglucosamine 2-Epimerase From E. Coli. [Escherichia coli],1F6D_B The Structure Of Udp-N-Acetylglucosamine 2-Epimerase From E. Coli. [Escherichia coli],1F6D_C The Structure Of Udp-N-Acetylglucosamine 2-Epimerase From E. Coli. [Escherichia coli],1F6D_D The Structure Of Udp-N-Acetylglucosamine 2-Epimerase From E. Coli. [Escherichia coli]
1VGV_A	3.34e-211	2	361	17	376	Crystalstructure of UDP-N-acetylglucosamine_2 epimerase [Escherichia coli],1VGV_B Crystal structure of UDP-N-acetylglucosamine_2 epimerase [Escherichia coli],1VGV_C Crystal structure of UDP-N-acetylglucosamine_2 epimerase [Escherichia coli],1VGV_D Crystal structure of UDP-N-acetylglucosamine_2 epimerase [Escherichia coli]
3DZC_A	5.85e-175	1	354	41	394	2.35Angstrom resolution structure of WecB (VC0917), a UDP-N-acetylglucosamine 2-epimerase from Vibrio cholerae. [Vibrio cholerae],3DZC_B 2.35 Angstrom resolution structure of WecB (VC0917), a UDP-N-acetylglucosamine 2-epimerase from Vibrio cholerae. [Vibrio cholerae]
6VLB_A	5.51e-150	1	360	16	374	Crystalstructure of ligand-free UDP-GlcNAc 2-epimerase from Neisseria meningitidis [Neisseria meningitidis Z2491],6VLB_B Crystal structure of ligand-free UDP-GlcNAc 2-epimerase from Neisseria meningitidis [Neisseria meningitidis Z2491],6VLC_A Crystal structure of UDP-GlcNAc 2-epimerase from Neisseria meningitidis bound to UDP-GlcNAc [Neisseria meningitidis Z2491],6VLC_B Crystal structure of UDP-GlcNAc 2-epimerase from Neisseria meningitidis bound to UDP-GlcNAc [Neisseria meningitidis Z2491],6VLC_C Crystal structure of UDP-GlcNAc 2-epimerase from Neisseria meningitidis bound to UDP-GlcNAc [Neisseria meningitidis Z2491],6VLC_D Crystal structure of UDP-GlcNAc 2-epimerase from Neisseria meningitidis bound to UDP-GlcNAc [Neisseria meningitidis Z2491]
5DLD_A	3.97e-148	1	354	25	378	CrystalStructure of a UDP-N-acetylglucosamine 2-epimerase from Burkholderia vietnamiensis complexed with UDP-GlcNAc and UDP [Burkholderia vietnamiensis G4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8ZAE3	6.70e-218	1	361	16	376	UDP-N-acetylglucosamine 2-epimerase OS=Yersinia pestis OX=632 GN=wecB PE=3 SV=1
Q8XAR8	6.70e-218	1	361	16	376	UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli O157:H7 OX=83334 GN=wecB PE=3 SV=1
P27828	5.49e-217	1	361	16	376	UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli (strain K12) OX=83333 GN=wecB PE=1 SV=2
Q9L6R5	1.17e-211	1	361	16	376	UDP-N-acetylglucosamine 2-epimerase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=wecB PE=3 SV=1
Q8Z388	1.94e-210	1	361	16	376	UDP-N-acetylglucosamine 2-epimerase OS=Salmonella typhi OX=90370 GN=wecB 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
1.000055	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002385_03556.