CAZyme Information: MGYG000002437_03340

Basic Information

• Species: Blautia hominis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia hominis
• CAZyme ID: MGYG000002437_03340
• CAZy Family: GT0
• CAZyme Description: UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
389	MGYG000002437_5|CGC2	44018.5	5.8402

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002437	5878941	Isolate	South Korea	Asia

• Gene Location: Start: 74921; End: 76090 Strand: -

Full Sequence      

MNYEDIKWKENGKLKLLIIVGTRPEIIRLAAVINKNRQYFDVILAHTGQNYDYNLNGVFF
KELKLDDPEVYLNAVGDDLGETCGNIIAQSYKLMVAIKPEAVLVLGDTNSCLSVIGAKRL
HIPIFHMEAGNRCKDECLPEETNRRIVDIISDVNMAYSEHARRYLADCGFPKERTYVTGS
PMAEVLYNNLAEIEESDIHVRLGLEKGKYILLSAHREENIDTEKNFLSLFKAINKMAEKY
DIPILYSCHPRSRKRLEQSGFKLDSRVIQHEPLGFHDYNCLQMNAFVVVSDSGTLPEESS
FFISVGHPFPAVCIRTSTERPEALDKACFILSGIDEKGLLQSVDTAVELNKAGDYGIPVP
DYIEENVSTKVVKIIQSYTGVVNKMVWRK

Enzyme Prediction     

No EC number prediction in MGYG000002437_03340.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0381	WecB	8.03e-133	11	389	1	382	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
cd03786	GTB_UDP-GlcNAc_2-Epimerase	8.91e-130	15	376	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	1.28e-89	36	375	4	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANT96561.1	3.52e-192	1	389	1	396
APZ79465.1	3.52e-192	1	389	1	396
AOP02734.1	6.20e-192	5	389	12	402
AOP02923.1	8.81e-192	5	389	12	402
AOP03494.1	9.72e-192	5	389	5	395

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4HWG_A	5.25e-103	14	389	10	384	Structureof UDP-N-acetylglucosamine 2-epimerase from Rickettsia bellii [Rickettsia bellii RML369-C]
4NEQ_A	2.36e-56	15	358	2	347	Thestructure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii [Methanocaldococcus jannaschii DSM 2661],4NES_A Crystal structure of Methanocaldococcus jannaschii UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP [Methanocaldococcus jannaschii DSM 2661]
5ENZ_A	1.63e-32	15	348	3	333	S.aureus MnaA-UDP co-structure [Staphylococcus aureus],5ENZ_B S. aureus MnaA-UDP co-structure [Staphylococcus aureus]
3BEO_A	2.43e-30	13	354	8	347	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	1.48e-29	13	341	3	328	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q6LZC4	3.52e-57	15	351	3	341	UDP-N-acetylglucosamine 2-epimerase OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=wecB PE=1 SV=1
Q58899	4.94e-57	14	358	1	347	UDP-N-acetylglucosamine 2-epimerase OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=wecB PE=1 SV=1
Q6M0B4	2.20e-51	14	377	1	356	UDP-N-acetylglucosamine 2-epimerase homolog OS=Methanococcus maripaludis (strain S2 / LL) OX=267377 GN=MMP0357 PE=1 SV=1
G3XD61	8.34e-44	14	347	1	327	UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=wbpI PE=1 SV=1
Q9X0C4	1.10e-31	14	341	2	329	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000081	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002437_03340.