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CAZyme Information: MGYG000000311_00443

You are here: Home > Sequence: MGYG000000311_00443

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 Veillonella sp900550175
Lineage Bacteria; Firmicutes_C; Negativicutes; Veillonellales; Veillonellaceae; Veillonella; Veillonella sp900550175
CAZyme ID MGYG000000311_00443
CAZy Family GT0
CAZyme Description UDP-N-acetylglucosamine 2-epimerase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
380 MGYG000000311_12|CGC1 42139.8 4.784
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000311 1913729 MAG Sweden Europe
Gene Location Start: 17511;  End: 18653  Strand: -

Full Sequence      Download help

MLKVMTIFGT  RPEAIKMAPL  VKALEAAPDM  EPIVTVTAQH  RDMLDQVLNL  FNITPDYDLN60
IMSQGQTLYD  VTNRALMGLK  DVLEEAKPDV  VLVHGDTTTT  FAGALASFYQ  EIPVGHVEAG120
LRTGDIYSPF  PEEMNRKLTG  SIATYHFAPT  ASSESNLKKE  NINTEHLYVT  GNTVIDALDT180
TVQDNYVFDD  AAINALDPEK  RTVLVTTHRR  ENLGEPMRHV  YQAIRDLINE  FKDIQVVFPV240
HKNPKVRQVV  QEELGSVERV  TLIDPLDYEP  FANLMAKSYL  ILTDSGGIQE  EAPALGKPVL300
VLRDTTERPE  AVEAGTVRLV  GTDKDAVHAA  AHELLSNAEA  YKLMSNSVNP  YGDGKASERI360
IQALRHEFLG  DSNRPERFGK  380

Enzyme Prediction      help

No EC number prediction in MGYG000000311_00443.

CDD Domains      download full data without filtering help

Created with Snap19385776951141331521711902092282472662853043233423611378WecB2368wecB3364GTB_UDP-GlcNAc_2-Epimerase22365Epimerase_268345GT4_PimA-like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0381 WecB 0.0 1 378 3 382
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236 wecB 0.0 2 368 1 365
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 7.95e-163 3 364 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 2.90e-150 22 365 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.
cd03801 GT4_PimA-like 1.71e-05 68 345 63 341
phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the 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. The members of this family are found mainly in certain bacteria and archaea.

CAZyme Hits      help

Created with Snap19385776951141331521711902092282472662853043233423613378BCZ44502.1|GT03368QES71705.1|GT03368ALB48231.2|GT03364QGH21225.1|GT03364ALP89282.1|GT0
Hit ID E-Value Query Start Query End Hit Start Hit End
BCZ44502.1 2.79e-154 3 378 5 380
QES71705.1 2.27e-153 3 368 5 370
ALB48231.2 2.27e-153 3 368 5 370
QGH21225.1 2.14e-151 3 364 5 366
ALP89282.1 2.14e-151 3 364 5 366

PDB Hits      download full data without filtering help

Created with Snap193857769511413315217119020922824726628530432334236123683BEO_A23784FKZ_A13795ENZ_A23781O6C_A33661F6D_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3BEO_A 2.09e-158 2 368 9 373
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 6.25e-156 2 378 4 377
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]
5ENZ_A 6.63e-150 1 379 1 376
S.aureus MnaA-UDP co-structure [Staphylococcus aureus],5ENZ_B S. aureus MnaA-UDP co-structure [Staphylococcus aureus]
1O6C_A 1.04e-149 2 378 4 377
Crystalstructure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis],1O6C_B Crystal structure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis]
1F6D_A 1.62e-143 3 366 2 371
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap19385776951141331521711902092282472662853043233423612378sp|P39131|MNAA_BACSU1378sp|Q9X0C4|Y1034_THEMA2366sp|Q8XAR8|WECB_ECO572366sp|P27828|WECB_ECOLI2365sp|Q9L6R5|WECB_SALTY
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P39131 2.59e-155 2 378 4 377
UDP-N-acetylglucosamine 2-epimerase OS=Bacillus subtilis (strain 168) OX=224308 GN=mnaA PE=1 SV=1
Q9X0C4 9.77e-155 1 378 1 377
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 3.07e-148 2 366 1 371
UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli O157:H7 OX=83334 GN=wecB PE=3 SV=1
P27828 3.07e-148 2 366 1 371
UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli (strain K12) OX=83333 GN=wecB PE=1 SV=2
Q9L6R5 5.79e-146 2 365 1 370
UDP-N-acetylglucosamine 2-epimerase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 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
1.000063 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000311_00443.