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CAZyme Information: MGYG000004413_00488

You are here: Home > Sequence: MGYG000004413_00488

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 CAG-488 sp003486665
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; CAG-488; CAG-488 sp003486665
CAZyme ID MGYG000004413_00488
CAZy Family GT0
CAZyme Description UDP-N-acetylglucosamine 2-epimerase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
368 MGYG000004413_25|CGC2 41478.39 5.2918
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004413 2138170 MAG Israel Asia
Gene Location Start: 8104;  End: 9210  Strand: +

Full Sequence      Download help

MKKIMLVFGT  RPEAIKMCPL  VNELKSRESL  ETIVCVTGQH  RQMLDQVLEA  FGVTPDYDLS60
VMKDKQTLFD  ITTNILNRIK  TVLEEVKPDV  VLVHGDTSTT  FVTALACFYL  QIPVGHVEAG120
LRTYNIYSPY  PEEFNRQAVS  IISQYNFAPT  ELSKQNLLKE  GKNAETIFVT  GNTAIDALKT180
TVREDYSHPE  LDWANGSKLI  VITAHRRENL  GEPMHHMFRA  IRRIMDDHPD  VKAIYPIHMN240
PVVRKAADEE  LGGCDRIHII  EPLEVLDFHN  FLAKSYLILT  DSGGIQEEAP  SLGKPVLVMR300
DTTERPEGIK  AGTLRLVGTD  ESTIYDSFKE  LLENKESYDT  MAHTSNPYGD  GFACRRIADI360
LENGHTDI368

Enzyme Prediction      help

No EC number prediction in MGYG000004413_00488.

CDD Domains      download full data without filtering help

Created with Snap18365573921101281471651842022202392572762943123313491363WecB3365wecB3362GTB_UDP-GlcNAc_2-Epimerase22362Epimerase_276298GT28_Beta-DGS-like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0381 WecB 0.0 1 363 3 370
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236 wecB 5.31e-180 3 365 2 365
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 4.05e-158 3 362 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 2.40e-154 22 362 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 0.002 76 298 86 292
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

Created with Snap18365573921101281471651842022202392572762943123313491362QTF54836.1|GT01362QLA08260.1|GT01362AUV68874.1|GT01362AUV66492.1|GT01362AMW24368.1|GT0
Hit ID E-Value Query Start Query End Hit Start Hit End
QTF54836.1 1.39e-206 1 362 1 362
QLA08260.1 7.39e-204 1 362 1 362
AUV68874.1 1.64e-149 1 362 1 362
AUV66492.1 1.64e-149 1 362 1 362
AMW24368.1 9.41e-149 1 362 1 362

PDB Hits      download full data without filtering help

Created with Snap183655739211012814716518420222023925727629431233134933613BEO_A33614FKZ_A33611O6C_A33633OT5_A13625ENZ_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3BEO_A 3.08e-169 3 361 10 369
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]
4FKZ_A 8.01e-168 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 5.50e-161 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]
3OT5_A 8.92e-154 3 363 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]
5ENZ_A 1.98e-148 1 362 1 362
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

Created with Snap18365573921101281471651842022202392572762943123313493361sp|P39131|MNAA_BACSU1361sp|Q9X0C4|Y1034_THEMA1362sp|P58600|EPSC_RALSO3361sp|P45360|Y2874_CLOAB1362sp|P52641|EPSC_RALSL
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P39131 3.31e-167 3 361 5 363
UDP-N-acetylglucosamine 2-epimerase OS=Bacillus subtilis (strain 168) OX=224308 GN=mnaA PE=1 SV=1
Q9X0C4 1.65e-135 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 4.56e-132 1 362 1 371
Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum (strain GMI1000) OX=267608 GN=epsC PE=3 SV=1
P45360 5.19e-131 3 361 5 367
Putative UDP-N-acetylglucosamine 2-epimerase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=CA_C2874 PE=3 SV=2
P52641 5.25e-131 1 362 1 371
Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum OX=305 GN=epsC PE=3 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
1.000036 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004413_00488.