CAZyme Information: MGYG000002323_00025

Basic Information

• Species: Escherichia sp000208585
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia sp000208585
• CAZyme ID: MGYG000002323_00025
• CAZy Family: GT0
• CAZyme Description: UDP-N-acetylglucosamine 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
376	MGYG000002323_1|CGC1	42318.63	6.1878

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002323	4514939	Isolate	not provided	not provided

• Gene Location: Start: 27110; End: 28240 Strand: +

Full Sequence      

MKVLTVFGTRPEAIKMAPLVHALAKDPFFEAKVCVTAQHREMLDQVLKLFSIVPDYDLNI
MQPGQGLTEITCRILEGLKPILAEFKPDVVLVHGDTTTTLATSLAAFYQRIPVGHVEAGL
RTGDLYSPWPEEANRTLTGHLAMYHFSPTETSRQNLLRENVADSRIFITGNTVIDALLWV
RDQVMSSDTLRSELAENYPFIDPNKKMILVTGHRRESFGRGFEEICHALAEIATTHQDIQ
IVYPVHLNPNVREPVNRILGHVKNVILIDPQEYLPFVWLMNHAWLILTDSGGIQEEAPSL
GKPVLVMRDTTERPEAVTAGTVRLVGTDKQRIVEEVTRLLKDENEYQTMSRAHNPYGDGQ
ACSRILEALKNNRISL

Enzyme Prediction     

No EC number prediction in MGYG000002323_00025.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0381	WecB	0.0	1	376	4	375	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236	wecB	0.0	1	373	1	365	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]
cd03786	GTB_UDP-GlcNAc_2-Epimerase	1.14e-169	2	370	1	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.
pfam02350	Epimerase_2	4.07e-154	21	370	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.
COG0707	MurG	2.71e-05	71	370	76	352	UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQN33861.1	2.02e-215	1	375	1	375
AZP48621.1	1.17e-214	1	375	1	375
AZP44285.1	1.17e-214	1	375	1	375
QBJ09996.1	1.17e-214	1	375	1	375
AZP53030.1	1.66e-214	1	375	1	375

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1F6D_A	3.37e-268	2	376	2	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	4.55e-268	2	376	2	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	2.13e-181	2	369	27	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]
5DLD_A	4.76e-158	2	375	11	384	CrystalStructure of a UDP-N-acetylglucosamine 2-epimerase from Burkholderia vietnamiensis complexed with UDP-GlcNAc and UDP [Burkholderia vietnamiensis G4]
6VLB_A	1.23e-157	1	374	1	373	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8XAR8	3.94e-278	1	376	1	376	UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli O157:H7 OX=83334 GN=wecB PE=3 SV=1
P27828	1.87e-276	1	376	1	376	UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli (strain K12) OX=83333 GN=wecB PE=1 SV=2
Q9L6R5	2.16e-250	1	376	1	376	UDP-N-acetylglucosamine 2-epimerase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=wecB PE=3 SV=1
Q8Z388	3.57e-249	1	376	1	376	UDP-N-acetylglucosamine 2-epimerase OS=Salmonella typhi OX=90370 GN=wecB PE=3 SV=1
Q8ZAE3	2.82e-223	1	376	1	376	UDP-N-acetylglucosamine 2-epimerase OS=Yersinia pestis OX=632 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
1.000065	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002323_00025.