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CAZyme Information: MGYG000004432_00176

You are here: Home > Sequence: MGYG000004432_00176

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA3263;
CAZyme ID MGYG000004432_00176
CAZy Family GT0
CAZyme Description UDP-N-acetylglucosamine 2-epimerase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
382 MGYG000004432_1|CGC2 42238.21 5.3128
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004432 2675051 MAG Israel Asia
Gene Location Start: 196941;  End: 198089  Strand: -

Full Sequence      Download help

MKTVMLVFGT  RPEAIKMAPL  VKELQSRPSE  FKTIVTVTGQ  HRQMLDQVLE  IFDIKPDYDL60
NIMKAGQDLT  DITCRVLTGM  RDLLQDVRPD  VILVHGDTTT  STATALAAFY  AHIPVGHVEA120
GLRTHNLESP  WPEEANRQLT  GRLAEYHFAP  TPLSKSNLLA  EGVDEKKITV  TGNTVIDALI180
SVKHRLDEDA  ALRNAETANL  LKAGYNLERL  DGSRRLVLIT  GHRRENFGEG  FRNICNAIKT240
LAEKFTDVDF  VYPMHLNPNV  RKPIAEILGD  SSARDNAFFI  EPLEYLSFVN  LMGKSDIVLT300
DSGGIQEEAP  GLGKPVLVMR  DTTERPEALE  AGTVKLVGTD  YDAIVSSVSE  LLTDREAYDK360
MSHAVNPYGD  GKACPRIADT  LR382

Enzyme Prediction      help

No EC number prediction in MGYG000004432_00176.

CDD Domains      download full data without filtering help

Created with Snap19385776951141331521711912102292482672863053243433621381WecB4382wecB4381GTB_UDP-GlcNAc_2-Epimerase22382Epimerase_2209382COG4370
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0381 WecB 1.09e-175 1 381 3 368
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236 wecB 9.23e-167 4 382 3 362
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 7.87e-146 4 381 2 364
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 7.89e-142 22 382 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.
COG4370 COG4370 2.57e-05 209 382 221 408
Uncharacterized protein [Function unknown].

CAZyme Hits      help

Created with Snap19385776951141331521711912102292482672863053243433624382QLK59446.1|GT04382QUT15423.1|GT04382QQN33861.1|GT04382AZP48621.1|GT04382AZP44285.1|GT0
Hit ID E-Value Query Start Query End Hit Start Hit End
QLK59446.1 3.26e-152 4 382 3 370
QUT15423.1 1.07e-150 4 382 3 370
QQN33861.1 1.52e-150 4 382 3 370
AZP48621.1 2.16e-150 4 382 3 370
AZP44285.1 2.16e-150 4 382 3 370

PDB Hits      download full data without filtering help

Created with Snap193857769511413315217119121022924826728630532434336213813DZC_A43815DLD_A43821F6D_A43821VGV_A43813BEO_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3DZC_A 7.84e-152 1 381 25 394
2.35Angstrom resolution structure of WecB (VC0917), a UDP-N-acetylglucosamine 2-epimerase from Vibrio cholerae. [Vibrio cholerae],3DZC_B 2.35 Angstrom resolution structure of WecB (VC0917), a UDP-N-acetylglucosamine 2-epimerase from Vibrio cholerae. [Vibrio cholerae]
5DLD_A 1.07e-148 4 381 12 378
CrystalStructure of a UDP-N-acetylglucosamine 2-epimerase from Burkholderia vietnamiensis complexed with UDP-GlcNAc and UDP [Burkholderia vietnamiensis G4]
1F6D_A 9.88e-148 4 382 3 370
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]
1VGV_A 1.30e-147 4 382 3 370
Crystalstructure of UDP-N-acetylglucosamine_2 epimerase [Escherichia coli],1VGV_B Crystal structure of UDP-N-acetylglucosamine_2 epimerase [Escherichia coli],1VGV_C Crystal structure of UDP-N-acetylglucosamine_2 epimerase [Escherichia coli],1VGV_D Crystal structure of UDP-N-acetylglucosamine_2 epimerase [Escherichia coli]
3BEO_A 7.36e-140 4 381 11 369
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap19385776951141331521711912102292482672863053243433621382sp|P58600|EPSC_RALSO1382sp|P52641|EPSC_RALSL4382sp|Q8XAR8|WECB_ECO574382sp|P27828|WECB_ECOLI4382sp|Q8ZAE3|WECB_YERPE
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P58600 1.31e-159 1 382 1 371
Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum (strain GMI1000) OX=267608 GN=epsC PE=3 SV=1
P52641 3.75e-159 1 382 1 371
Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum OX=305 GN=epsC PE=3 SV=2
Q8XAR8 1.31e-152 4 382 3 370
UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli O157:H7 OX=83334 GN=wecB PE=3 SV=1
P27828 1.86e-152 4 382 3 370
UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli (strain K12) OX=83333 GN=wecB PE=1 SV=2
Q8ZAE3 1.75e-150 4 382 3 370
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
1.000065 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004432_00176.