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CAZyme Information: MGYG000004725_00348

You are here: Home > Sequence: MGYG000004725_00348

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 UBA9475 sp900554075
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA9475; UBA9475 sp900554075
CAZyme ID MGYG000004725_00348
CAZy Family GT0
CAZyme Description UDP-N-acetylglucosamine 2-epimerase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
380 MGYG000004725_3|CGC1 42157.33 5.2999
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004725 2206830 MAG Denmark Europe
Gene Location Start: 33065;  End: 34207  Strand: +

Full Sequence      Download help

MKKVMTVFGT  RPEAIKMAPL  VQELERRAGL  ESVCCVTAQH  RQMLDSVLGA  FSLTPDFDLD60
IMEPRQSLYT  ITSKALLGME  RVLQDAKPDL  VLVHGDTSTT  FAGALAAFYA  QVPVGHVEAG120
LRTYDRYSPF  PEEMNRTLTG  DLAALHFCPT  AANRENLRRE  GITKGVYLTG  NTVIDALGTT180
VRQDFVFQTP  LLNELDYEKR  KVILVTCHRR  ENYGAPMEHI  MSALRRLAVD  CPEAELVYPV240
HLSPVVQEVA  HKYLDGIENV  HLIAPLDVLE  MHNLMARAYL  VMTDSGGLQE  EAPALGKPVL300
VLRRETERPE  AVAAGTVRLA  GTEEEQVYAM  GRTLLADKNE  YDKMAHAVNP  YGDGRACCRI360
ADAIESYFGL  RDGAVEEWHG  380

Enzyme Prediction      help

No EC number prediction in MGYG000004725_00348.

CDD Domains      download full data without filtering help

Created with Snap19385776951141331521711902092282472662853043233423611378WecB3368wecB3365GTB_UDP-GlcNAc_2-Epimerase26365Epimerase_274367MurG
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 1.89e-169 3 368 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 6.65e-150 3 365 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 3.25e-144 26 365 4 336
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.
COG0707 MurG 2.96e-06 74 367 78 354
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Created with Snap19385776951141331521711902092282472662853043233423612378QGH21225.1|GT02378ALP89282.1|GT02378QJU45537.1|GT02378AOR92965.1|GT02378APF24762.1|GT0
Hit ID E-Value Query Start Query End Hit Start Hit End
QGH21225.1 4.47e-158 2 378 4 380
ALP89282.1 4.47e-158 2 378 4 380
QJU45537.1 4.47e-158 2 378 4 380
AOR92965.1 4.47e-158 2 378 4 380
APF24762.1 4.47e-158 2 378 4 380

PDB Hits      download full data without filtering help

Created with Snap193857769511413315217119020922824726628530432334236133804FKZ_A33683BEO_A33801O6C_A13705ENZ_A13643DZC_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
4FKZ_A 1.39e-147 3 380 5 379
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]
3BEO_A 2.06e-146 3 368 10 373
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]
1O6C_A 4.61e-141 3 380 5 379
Crystalstructure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis],1O6C_B Crystal structure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis]
5ENZ_A 1.94e-134 1 370 1 367
S.aureus MnaA-UDP co-structure [Staphylococcus aureus],5ENZ_B S. aureus MnaA-UDP co-structure [Staphylococcus aureus]
3DZC_A 3.01e-131 1 364 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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap19385776951141331521711902092282472662853043233423611376sp|Q9X0C4|Y1034_THEMA3378sp|P45360|Y2874_CLOAB3380sp|P39131|MNAA_BACSU3367sp|Q9L6R5|WECB_SALTY1368sp|P52641|EPSC_RALSL
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9X0C4 3.86e-159 1 376 1 376
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
P45360 2.51e-154 3 378 5 381
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
P39131 5.76e-147 3 380 5 379
UDP-N-acetylglucosamine 2-epimerase OS=Bacillus subtilis (strain 168) OX=224308 GN=mnaA PE=1 SV=1
Q9L6R5 1.69e-135 3 367 2 372
UDP-N-acetylglucosamine 2-epimerase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=wecB PE=3 SV=1
P52641 6.59e-135 1 368 1 374
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
1.000066 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004725_00348.