CAZyme Information: MGYG000003009_00198

Basic Information

• Species: Oribacterium sinus
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Oribacterium; Oribacterium sinus
• CAZyme ID: MGYG000003009_00198
• CAZy Family: GT0
• CAZyme Description: UDP-N-acetylglucosamine 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
281		32049.26	5.1096

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003009	1309457	MAG	United States	North America

• Gene Location: Start: 5638; End: 6483 Strand: -

Full Sequence      

MVHGDTTTTFATALACFYLQIPVGHVEAGLRTYNIYSPYPEEFNRQAVSILSEYNFAPTP
LSRDNLLHEGCRPEKIYVTGNTVIDAMKHTVKDEYKHPELEWVGQSKLIFITAHRRENLG
KPMHQMFRAIRRVLDEHEDCKAIYPIHMNPIVREAAEQELSGCDRIHIIEPIEVVDCHNF
EARSFLCLTDSGGIQEECPSYGVPVLVMRDTTERPEGVTSGTLRLVGTDEETIYNNFKLL
LENKEEYEKMSKACNPYGDGHACERIADILEGKDFTPWHST

Enzyme Prediction     

No EC number prediction in MGYG000003009_00198.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0381	WecB	6.27e-125	1	271	97	369	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236	wecB	4.97e-120	1	270	91	361	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	1.26e-109	1	271	71	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	4.10e-101	1	271	93	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTF54836.1	3.12e-145	1	271	92	362
QLA08260.1	5.43e-141	1	271	92	362
AVH46190.1	1.10e-109	1	271	92	362
AMW24368.1	3.14e-109	1	271	92	362
AUV68874.1	3.14e-109	1	271	92	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3BEO_A	1.52e-122	1	270	100	369	AStructural Basis for the allosteric regulation of non-hydrolyzing UDP-GlcNAc 2-epimerases [Bacillus anthracis],3BEO_B A Structural Basis for the allosteric regulation of non-hydrolyzing UDP-GlcNAc 2-epimerases [Bacillus anthracis]
4FKZ_A	1.34e-121	1	270	94	363	Crystalstructure of Bacillus subtilis UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP [Bacillus subtilis subsp. subtilis str. 168],4FKZ_B Crystal structure of Bacillus subtilis UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP [Bacillus subtilis subsp. subtilis str. 168]
1O6C_A	2.04e-118	1	270	94	363	Crystalstructure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis],1O6C_B Crystal structure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis]
3OT5_A	1.52e-111	1	271	119	389	2.2Angstrom Resolution Crystal Structure of putative UDP-N-acetylglucosamine 2-epimerase from Listeria monocytogenes [Listeria monocytogenes EGD-e],3OT5_B 2.2 Angstrom Resolution Crystal Structure of putative UDP-N-acetylglucosamine 2-epimerase from Listeria monocytogenes [Listeria monocytogenes EGD-e],3OT5_C 2.2 Angstrom Resolution Crystal Structure of putative UDP-N-acetylglucosamine 2-epimerase from Listeria monocytogenes [Listeria monocytogenes EGD-e],3OT5_D 2.2 Angstrom Resolution Crystal Structure of putative UDP-N-acetylglucosamine 2-epimerase from Listeria monocytogenes [Listeria monocytogenes EGD-e]
5ENZ_A	5.21e-108	1	271	92	362	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
P39131	5.62e-121	1	270	94	363	UDP-N-acetylglucosamine 2-epimerase OS=Bacillus subtilis (strain 168) OX=224308 GN=mnaA PE=1 SV=1
Q9X0C4	1.92e-98	1	270	92	364	Putative UDP-N-acetylglucosamine 2-epimerase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=TM_1034 PE=3 SV=1
P45360	1.10e-96	1	270	94	367	Putative UDP-N-acetylglucosamine 2-epimerase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=CA_C2874 PE=3 SV=2
Q8XAR8	1.90e-87	1	273	91	372	UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli O157:H7 OX=83334 GN=wecB PE=3 SV=1
P27828	7.63e-87	1	273	91	372	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
0.764147	0.234214	0.000906	0.000259	0.000183	0.000299

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003009_00198.