Species | ||||||||||||
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Lineage | Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Atopobiaceae; UMGS1418; | |||||||||||
CAZyme ID | MGYG000002094_01354 | |||||||||||
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: 404; End: 1357 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0381 | WecB | 1.43e-108 | 2 | 316 | 70 | 382 | UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]. |
cd03786 | GTB_UDP-GlcNAc_2-Epimerase | 1.79e-108 | 2 | 303 | 66 | 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 | 9.16e-78 | 2 | 302 | 44 | 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 | 2.38e-163 | 1 | 316 | 88 | 402 |
AOP02687.1 | 2.38e-163 | 1 | 316 | 88 | 402 |
AOP03732.1 | 2.38e-163 | 1 | 316 | 88 | 402 |
AOP02662.1 | 2.38e-163 | 1 | 316 | 88 | 402 |
AOP03614.1 | 2.38e-163 | 1 | 316 | 88 | 402 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4HWG_A | 2.62e-86 | 4 | 316 | 74 | 384 | Structureof UDP-N-acetylglucosamine 2-epimerase from Rickettsia bellii [Rickettsia bellii RML369-C] |
4NEQ_A | 5.10e-38 | 6 | 269 | 68 | 334 | 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 | 1.27e-30 | 6 | 309 | 65 | 368 | S.aureus MnaA-UDP co-structure [Staphylococcus aureus],5ENZ_B S. aureus MnaA-UDP co-structure [Staphylococcus aureus] |
6VLB_A | 2.39e-24 | 4 | 274 | 66 | 340 | Crystalstructure of ligand-free UDP-GlcNAc 2-epimerase from Neisseria meningitidis [Neisseria meningitidis Z2491],6VLB_B Crystal structure of ligand-free UDP-GlcNAc 2-epimerase from Neisseria meningitidis [Neisseria meningitidis Z2491],6VLC_A Crystal structure of UDP-GlcNAc 2-epimerase from Neisseria meningitidis bound to UDP-GlcNAc [Neisseria meningitidis Z2491],6VLC_B Crystal structure of UDP-GlcNAc 2-epimerase from Neisseria meningitidis bound to UDP-GlcNAc [Neisseria meningitidis Z2491],6VLC_C Crystal structure of UDP-GlcNAc 2-epimerase from Neisseria meningitidis bound to UDP-GlcNAc [Neisseria meningitidis Z2491],6VLC_D Crystal structure of UDP-GlcNAc 2-epimerase from Neisseria meningitidis bound to UDP-GlcNAc [Neisseria meningitidis Z2491] |
1F6D_A | 1.29e-21 | 2 | 304 | 64 | 371 | TheStructure Of Udp-N-Acetylglucosamine 2-Epimerase From E. Coli. [Escherichia coli],1F6D_B The Structure Of Udp-N-Acetylglucosamine 2-Epimerase From E. Coli. [Escherichia coli],1F6D_C The Structure Of Udp-N-Acetylglucosamine 2-Epimerase From E. Coli. [Escherichia coli],1F6D_D The Structure Of Udp-N-Acetylglucosamine 2-Epimerase From E. Coli. [Escherichia coli] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q6LZC4 | 1.51e-40 | 6 | 282 | 67 | 346 | UDP-N-acetylglucosamine 2-epimerase OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=wecB PE=1 SV=1 |
Q58899 | 4.49e-38 | 6 | 269 | 68 | 334 | 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 | 8.50e-30 | 6 | 269 | 67 | 327 | UDP-N-acetylglucosamine 2-epimerase homolog OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=MMP0357 PE=1 SV=1 |
Q9X0C4 | 3.18e-29 | 4 | 310 | 67 | 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 |
G3XD61 | 5.70e-28 | 2 | 273 | 65 | 327 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000069 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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