CAZyme Information: MGYG000001252_01378

Basic Information

• Species: Catenibacillus sp900557175
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Catenibacillus; Catenibacillus sp900557175
• CAZyme ID: MGYG000001252_01378
• CAZy Family: GT0
• CAZyme Description: UDP-N-acetylglucosamine 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
265		29948.34	5.4985

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001252	2417693	MAG	Austria	Europe

• Gene Location: Start: 4734; End: 5531 Strand: -

Full Sequence      

MEAGNRCKDECLPEETNRRIVDVISDVNLCYSEFARKYLADTGLPKERTYMTGSPMAEVL
RGNLDKIQSSDVLERMGLEKDKYILLSAHREENIDTEKNFTSLFKAINALAEKYDMPILY
SCHPRSKNRLDKSGFKLNPRVRVNEPLGFNDYNCLQMNALAIVSDSGTLPEESSFYLSIG
HPIAAVCIRTSTERPEALEAGDFILAGITTKELLNATDMAIEMKQKGVFGKPCPDYVDET
VSMKVVRIIQGYVNVVNKMVWRKEQ

Enzyme Prediction     

No EC number prediction in MGYG000001252_01378.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03786	GTB_UDP-GlcNAc_2-Epimerase	9.55e-81	1	250	118	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.
COG0381	WecB	4.59e-78	1	264	122	383	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
pfam02350	Epimerase_2	7.21e-53	1	249	96	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	6.84e-175	1	265	140	404
AOP02687.1	6.84e-175	1	265	140	404
AOP03732.1	6.84e-175	1	265	140	404
AOP02662.1	6.84e-175	1	265	140	404
AOP03614.1	6.84e-175	1	265	140	404

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4HWG_A	2.44e-62	1	263	123	384	Structureof UDP-N-acetylglucosamine 2-epimerase from Rickettsia bellii [Rickettsia bellii RML369-C]
4NEQ_A	2.12e-31	1	230	116	349	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	5.70e-24	1	258	117	370	S.aureus MnaA-UDP co-structure [Staphylococcus aureus],5ENZ_B S. aureus MnaA-UDP co-structure [Staphylococcus aureus]
3BEO_A	1.18e-21	1	254	125	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]
4FKZ_A	3.86e-19	1	225	119	345	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q58899	3.77e-31	1	230	116	349	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
Q6LZC4	2.79e-28	1	222	115	338	UDP-N-acetylglucosamine 2-epimerase OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=wecB PE=1 SV=1
Q9X0C4	2.17e-19	1	249	117	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
P39131	2.00e-18	1	225	119	345	UDP-N-acetylglucosamine 2-epimerase OS=Bacillus subtilis (strain 168) OX=224308 GN=mnaA PE=1 SV=1
Q6M0B4	2.26e-18	1	214	115	324	UDP-N-acetylglucosamine 2-epimerase homolog OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=MMP0357 PE=1 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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001252_01378.