CAZyme Information: MGYG000002959_01365

Basic Information

• Species: Peptoniphilus_A lacydonensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Peptoniphilus_A; Peptoniphilus_A lacydonensis
• CAZyme ID: MGYG000002959_01365
• CAZy Family: GT0
• CAZyme Description: UDP-N-acetylglucosamine 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
367	MGYG000002959_7|CGC1	41635.81	5.732

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002959	1622414	MAG	United States	North America

• Gene Location: Start: 29022; End: 30125 Strand: +

Full Sequence      

MKVLFVFGTRPEGIKMAPIIKEIEKRNNIESYTCVTGQHREMLDQVLEIFDIKPDYDLNI
FKNGQSLTDVTTKTLQGLEKILDELKPDILLVQGDTTTVFAAALAAFYKKIKIGHVEAGL
RSGNLYSPYPEEANRKLTGVIANYHFAPTNSNKENLLREGYDEKNIFITGNTVIDALKYS
VKEDFVFDDEILNNLDYNKDVVLLTAHRRENWGEPMENIFSSIRRVVLERENLEIVFPIH
LNPIVRNTAKKYFSDLDRVHMIEPLSYMPFSNLMSRVKFVVTDSGGVQEEAPALGKPVLV
LRNETERMEGVKAKTAKLVGTDSKNVYENIIKLLDDKKLYDQMAKAVNPYGDGHAATKIV
DILEGMN

Enzyme Prediction     

No EC number prediction in MGYG000002959_01365.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR00236	wecB	1.22e-177	1	363	1	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]
COG0381	WecB	1.41e-177	1	364	4	369	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
cd03786	GTB_UDP-GlcNAc_2-Epimerase	7.68e-161	2	364	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	2.45e-155	21	364	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.
PRK13609	PRK13609	8.82e-06	18	364	48	367	diacylglycerol glucosyltransferase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGH21225.1	1.39e-153	2	363	5	366
ALP89282.1	1.39e-153	2	363	5	366
QJU45537.1	1.39e-153	2	363	5	366
AOR92965.1	1.39e-153	2	363	5	366
APF24762.1	1.39e-153	2	363	5	366

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4FKZ_A	6.95e-147	1	363	4	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]
3BEO_A	4.81e-144	1	367	9	374	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]
1O6C_A	1.42e-141	1	363	4	363	Crystalstructure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis],1O6C_B Crystal structure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis]
3OT5_A	3.60e-138	1	360	28	385	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	8.51e-135	2	361	3	359	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
P45360	1.02e-152	1	363	4	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
Q9X0C4	2.87e-148	1	360	2	361	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
P39131	2.89e-146	1	363	4	363	UDP-N-acetylglucosamine 2-epimerase OS=Bacillus subtilis (strain 168) OX=224308 GN=mnaA PE=1 SV=1
Q9L6R5	2.79e-133	1	364	1	370	UDP-N-acetylglucosamine 2-epimerase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=wecB PE=3 SV=1
P27828	1.13e-132	1	364	1	370	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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002959_01365.