Species | Holdemania sp900120005 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Holdemania; Holdemania sp900120005 | |||||||||||
CAZyme ID | MGYG000002779_02285 | |||||||||||
CAZy Family | GT0 | |||||||||||
CAZyme Description | UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 28844; End: 30031 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03786 | GTB_UDP-GlcNAc_2-Epimerase | 1.07e-132 | 20 | 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. |
COG0381 | WecB | 1.63e-132 | 16 | 393 | 1 | 381 | UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]. |
pfam02350 | Epimerase_2 | 2.14e-90 | 42 | 380 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AOP03843.1 | 3.17e-191 | 1 | 393 | 3 | 401 |
AOP02687.1 | 3.17e-191 | 1 | 393 | 3 | 401 |
AOP03732.1 | 3.17e-191 | 1 | 393 | 3 | 401 |
AOP02662.1 | 3.17e-191 | 1 | 393 | 3 | 401 |
AOP03614.1 | 3.17e-191 | 1 | 393 | 3 | 401 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4HWG_A | 4.39e-106 | 12 | 392 | 3 | 382 | Structureof UDP-N-acetylglucosamine 2-epimerase from Rickettsia bellii [Rickettsia bellii RML369-C] |
4NEQ_A | 5.42e-51 | 20 | 349 | 2 | 335 | 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] |
3BEO_A | 1.18e-35 | 18 | 349 | 8 | 337 | 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 | 5.05e-32 | 18 | 346 | 3 | 328 | 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] |
3OT5_A | 6.41e-32 | 10 | 346 | 17 | 353 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q6LZC4 | 1.02e-53 | 20 | 355 | 3 | 340 | UDP-N-acetylglucosamine 2-epimerase OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=wecB PE=1 SV=1 |
Q58899 | 1.17e-51 | 19 | 349 | 1 | 335 | 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 | 4.09e-49 | 19 | 382 | 1 | 356 | UDP-N-acetylglucosamine 2-epimerase homolog OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=MMP0357 PE=1 SV=1 |
G3XD61 | 2.90e-40 | 19 | 359 | 1 | 334 | 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 | 9.14e-33 | 19 | 346 | 2 | 329 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000043 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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