CAZyme Information: MGYG000003409_00472

Basic Information

• Species: CAG-110 sp900544945
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp900544945
• CAZyme ID: MGYG000003409_00472
• CAZy Family: GT0
• CAZyme Description: UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
391	MGYG000003409_45|CGC1	43877.25	6.3677

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003409	2672842	MAG	Fiji	Oceania

• Gene Location: Start: 98953; End: 100128 Strand: +

Full Sequence      

MADYSNISFRNNGKLKLLIIVGTRPEIIRLSAVINKTRRYFDVILAHTGQNYDYNLNGVF
FHDLELADPEVYLNAVGADLGETMGNIIAESYKLMVRIQPDAVLVLGDTNSCLSVIGAKR
LHIPIFHMEAGNRCKDECLPEETNRRIVDIISDVNMAYSEHARRYLADTGLPKERTYVTG
SPMAEVLHQNLSKIEASDIHARLGLQKGKYILLSAHREENIDTEKNFLSLFNAINAMAEK
YDMPILYSCHPRSKKRLAQSGFVLDKRVIAHEPLGFHDYNCLQMNAFCVVSDSGTLPEES
SFFTSAGHPFPAVCIRTSTERPEALDKGCFILSGIDEKGLLQAVDVAVEMNRNGDLGIPV
PDYRDENVSDKVVKIIQSYTGVVDKMVWRKF

Enzyme Prediction     

No EC number prediction in MGYG000003409_00472.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0381	WecB	3.83e-135	12	390	1	382	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
cd03786	GTB_UDP-GlcNAc_2-Epimerase	6.39e-134	16	377	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	8.57e-94	38	376	5	335	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOP03843.1	6.35e-190	6	390	12	402
AOP02687.1	6.35e-190	6	390	12	402
AOP03732.1	6.35e-190	6	390	12	402
AOP02662.1	6.35e-190	6	390	12	402
AOP03614.1	6.35e-190	6	390	12	402

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4HWG_A	9.55e-107	15	391	10	385	Structureof UDP-N-acetylglucosamine 2-epimerase from Rickettsia bellii [Rickettsia bellii RML369-C]
4NEQ_A	5.49e-59	16	353	2	343	Thestructure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii [Methanocaldococcus jannaschii DSM 2661],4NES_A Crystal structure of Methanocaldococcus jannaschii UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP [Methanocaldococcus jannaschii DSM 2661]
5ENZ_A	1.26e-33	16	383	3	368	S.aureus MnaA-UDP co-structure [Staphylococcus aureus],5ENZ_B S. aureus MnaA-UDP co-structure [Staphylococcus aureus]
4FKZ_A	5.52e-29	14	381	3	368	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	2.25e-28	14	379	8	372	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q6LZC4	8.08e-60	16	353	3	342	UDP-N-acetylglucosamine 2-epimerase OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=wecB PE=1 SV=1
Q58899	8.08e-60	15	353	1	343	UDP-N-acetylglucosamine 2-epimerase OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=wecB PE=1 SV=1
Q6M0B4	7.69e-48	15	344	1	327	UDP-N-acetylglucosamine 2-epimerase homolog OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=MMP0357 PE=1 SV=1
G3XD61	5.29e-39	15	362	1	333	UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=wbpI PE=1 SV=1
Q9X0C4	2.30e-33	15	384	2	372	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

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
1.000080	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003409_00472.