CAZyme Information: MGYG000000236_00524

Basic Information

• Species: Bacteroides fragilis_A
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides fragilis_A
• CAZyme ID: MGYG000000236_00524
• CAZy Family: GT0
• CAZyme Description: UDP-N-acetylglucosamine 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
385	MGYG000000236_2|CGC8	43883.82	6.1131

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000236	5355078	Isolate	China	Asia

• Gene Location: Start: 198619; End: 199776 Strand: +

Full Sequence      

MKKVMLVFGTRPEAIKMCPLIMELNKAFDNFETIVCVTGQHREMLDQVLGFFEIIPDVDL
NIMKGGQDLYDITSRVLIGMRDALNKYAPDIVIVHGDTTTTFAASLAAFYQKIPVAHVEA
GLRTYNLYSPWPEEINRQLASRICQYHFAPTSLSRENLLHENIESKNILVTGNTVIDALH
IVVDKINTNYDLEKNLALNLLRVGYDVQRLQNGRKMILITGHRRENFGDGFVNICKAIRT
LSRRYETVDFVYPMHLNPNVRTPIYQIFKDEKLSNVFFIEPLEYLSFIFLMEKSCIVMTD
SGGIQEEAPSLGKPVLVMRDTTERPEAIEAGTVKLVGTDCTKIVEEVSLLLENELYYTQM
NRATNPYGDGNASKRIVEFLKMRLP

Enzyme Prediction     

No EC number prediction in MGYG000000236_00524.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0381	WecB	0.0	1	381	3	369	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236	wecB	1.80e-173	3	381	2	362	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	2.56e-156	3	381	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	1.27e-152	29	381	6	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.
cd03794	GT4_WbuB-like	0.009	42	363	53	372	Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQN33861.1	4.56e-148	3	381	2	370
AZP48621.1	2.62e-147	3	381	2	370
AZP44285.1	2.62e-147	3	381	2	370
QBJ09996.1	2.62e-147	3	381	2	370
AZP53030.1	3.71e-147	3	381	2	370

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DZC_A	4.36e-152	1	380	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]
6VLB_A	2.39e-145	3	384	2	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]
1F6D_A	4.83e-144	3	381	2	370	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	6.35e-144	3	381	2	370	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]
5DLD_A	1.71e-138	3	380	11	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
P27828	1.12e-149	3	381	2	370	UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli (strain K12) OX=83333 GN=wecB PE=1 SV=2
Q8XAR8	1.12e-149	3	381	2	370	UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli O157:H7 OX=83334 GN=wecB PE=3 SV=1
Q8ZAE3	1.29e-148	3	381	2	370	UDP-N-acetylglucosamine 2-epimerase OS=Yersinia pestis OX=632 GN=wecB PE=3 SV=1
P52641	2.52e-148	1	381	1	371	Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum OX=305 GN=epsC PE=3 SV=2
P58600	3.57e-148	1	381	1	371	Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum (strain GMI1000) OX=267608 GN=epsC 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
1.000066	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000236_00524.