CAZyme Information: MGYG000003399_03498

Basic Information

• Species: Serratia ureilytica
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Serratia; Serratia ureilytica
• CAZyme ID: MGYG000003399_03498
• CAZy Family: GT0
• CAZyme Description: UDP-N-acetylglucosamine 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
370	MGYG000003399_21|CGC4	41026.14	5.4286

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003399	5050953	MAG	United States	North America

• Gene Location: Start: 177368; End: 178480 Strand: -

Full Sequence      

MLKKIMCVVGTRPEAIKMAPVIKALHASGEFDVCVLATAQHRDLLDQAFQLFEIEADYDL
NVMTPGQTLPELTARLMTSIDRTLEEAAPDLVIAQGDTTTVFVTSLACFYKKVPFAHLEA
GLRTHDLYSPFPEEANRILAGHLARLHFAPTEVSKSNLLREGIPAEHIHVTGNTVIDALL
TTAQKTFDIGVDIPQDARMLLITSHRRENFGQPIVNICNAALELIEKYSDIYILFPVHPN
PNVREVTDRLLKEHERIKLVSPFDYGPFVAAMKNAYLILSDSGGVQEEAPALGKPVLVLR
RDTERPEAVSEGVVKLIGTEQADIVREASLLLDSPQAYQKMAKGSSPYGDGESSQRIVRI
VRNFFTEQCQ

Enzyme Prediction     

No EC number prediction in MGYG000003399_03498.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0381	WecB	5.42e-171	3	366	4	373	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236	wecB	6.05e-169	4	365	2	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	8.75e-153	4	361	1	364	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	9.07e-140	23	362	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.
pfam13579	Glyco_trans_4_4	1.72e-05	21	173	10	157	Glycosyl transferase 4-like domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYN12150.1	2.35e-161	4	369	2	366
QQN33861.1	1.67e-129	4	368	2	376
AZP48621.1	3.36e-129	4	368	2	376
AZP44285.1	3.36e-129	4	368	2	376
QBJ09996.1	3.36e-129	4	368	2	376

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6VLB_A	6.47e-124	4	361	2	368	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]
3DZC_A	1.10e-123	2	361	25	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]
1F6D_A	1.61e-123	4	363	2	371	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	2.10e-123	4	363	2	371	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]
5ENZ_A	4.37e-123	2	368	1	371	S.aureus MnaA-UDP co-structure [Staphylococcus aureus],5ENZ_B S. aureus MnaA-UDP co-structure [Staphylococcus aureus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P58600	6.96e-132	2	365	1	374	Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum (strain GMI1000) OX=267608 GN=epsC PE=3 SV=1
P52641	1.14e-130	2	365	1	374	Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum OX=305 GN=epsC PE=3 SV=2
Q9L6R5	2.71e-129	4	364	2	372	UDP-N-acetylglucosamine 2-epimerase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=wecB PE=3 SV=1
Q8Z388	3.85e-129	4	364	2	372	UDP-N-acetylglucosamine 2-epimerase OS=Salmonella typhi OX=90370 GN=wecB PE=3 SV=1
P27828	2.20e-128	4	363	2	371	UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli (strain K12) OX=83333 GN=wecB PE=1 SV=2

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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003399_03498.