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CAZyme Information: MGYG000001842_00268

You are here: Home > Sequence: MGYG000001842_00268

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Collinsella sp900758375
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900758375
CAZyme ID MGYG000001842_00268
CAZy Family GT0
CAZyme Description UDP-N-acetylglucosamine 2-epimerase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
365 MGYG000001842_3|CGC1 40813.74 6.3388
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001842 2095913 MAG Denmark Europe
Gene Location Start: 92957;  End: 94054  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001842_00268.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR00236 wecB 1.79e-178 1 361 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 1.25e-175 1 363 4 370
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
cd03786 GTB_UDP-GlcNAc_2-Epimerase 1.32e-152 2 362 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 3.68e-150 21 362 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.
cd17507 GT28_Beta-DGS-like 3.00e-05 78 345 88 343
beta-diglucosyldiacylglycerol synthase and similar proteins. beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QLA08260.1 1.20e-185 2 361 3 361
QTF54836.1 7.93e-182 2 361 3 361
QIL47435.1 3.16e-141 2 361 5 365
AUV68874.1 4.62e-141 2 357 3 357
AUV66492.1 4.62e-141 2 357 3 357

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4FKZ_A 5.82e-155 1 361 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]
3OT5_A 5.27e-152 2 363 29 390
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]
3BEO_A 5.72e-152 1 361 9 369
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 3.94e-148 1 361 4 363
Crystalstructure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis],1O6C_B Crystal structure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis]
5ENZ_A 1.11e-139 2 359 3 359
S.aureus MnaA-UDP co-structure [Staphylococcus aureus],5ENZ_B S. aureus MnaA-UDP co-structure [Staphylococcus aureus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P39131 2.41e-154 1 361 4 363
UDP-N-acetylglucosamine 2-epimerase OS=Bacillus subtilis (strain 168) OX=224308 GN=mnaA PE=1 SV=1
Q8ZAE3 1.49e-127 1 361 1 369
UDP-N-acetylglucosamine 2-epimerase OS=Yersinia pestis OX=632 GN=wecB PE=3 SV=1
Q9X0C4 7.37e-126 2 361 3 364
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
Q8XAR8 7.92e-125 1 365 1 373
UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli O157:H7 OX=83334 GN=wecB PE=3 SV=1
P27828 2.26e-124 1 365 1 373
UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli (strain K12) OX=83333 GN=wecB PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000072 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001842_00268.