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CAZyme Information: MGYG000001155_01391

You are here: Home > Sequence: MGYG000001155_01391

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 UBA738 sp004557735
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA738; UBA738 sp004557735
CAZyme ID MGYG000001155_01391
CAZy Family GT0
CAZyme Description UDP-N-acetylglucosamine 2-epimerase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
372 MGYG000001155_232|CGC1 41529.4 6.1422
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001155 1976528 MAG Austria Europe
Gene Location Start: 13363;  End: 14481  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001155_01391.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0381 WecB 9.64e-172 1 361 3 368
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236 wecB 2.13e-168 3 361 2 361
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]
cd03786 GTB_UDP-GlcNAc_2-Epimerase 4.81e-147 3 361 1 364
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 1.48e-139 22 361 1 335
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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QTF54836.1 2.01e-193 1 361 1 361
QLA08260.1 1.23e-182 1 361 1 361
AUV68874.1 9.65e-145 1 361 1 361
AUV66492.1 9.65e-145 1 361 1 361
AMW24368.1 5.54e-144 1 361 1 361

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3BEO_A 9.44e-160 3 363 10 371
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]
3OT5_A 9.73e-152 3 371 29 399
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]
4FKZ_A 1.66e-151 3 361 5 363
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]
1O6C_A 3.91e-145 3 361 5 363
Crystalstructure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis],1O6C_B Crystal structure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis]
5ENZ_A 3.81e-142 1 361 1 361
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 6.87e-151 3 361 5 363
UDP-N-acetylglucosamine 2-epimerase OS=Bacillus subtilis (strain 168) OX=224308 GN=mnaA PE=1 SV=1
Q9X0C4 6.26e-134 1 361 1 364
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
P58600 1.73e-130 1 361 1 370
Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum (strain GMI1000) OX=267608 GN=epsC PE=3 SV=1
P52641 2.82e-129 1 361 1 370
Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum OX=305 GN=epsC PE=3 SV=2
Q8ZAE3 1.45e-124 3 361 2 369
UDP-N-acetylglucosamine 2-epimerase OS=Yersinia pestis OX=632 GN=wecB PE=3 SV=1

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
1.000048 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001155_01391.