Species | Paramuribaculum sp900759915 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp900759915 | |||||||||||
CAZyme ID | MGYG000004720_01387 | |||||||||||
CAZy Family | GT9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 10190; End: 11182 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT9 | 68 | 308 | 2.2e-34 | 0.9733333333333334 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03789 | GT9_LPS_heptosyltransferase | 8.51e-50 | 2 | 325 | 3 | 277 | lipopolysaccharide heptosyltransferase and similar proteins. Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and 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. |
COG0859 | RfaF | 8.92e-39 | 1 | 319 | 4 | 322 | ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis]. |
pfam01075 | Glyco_transf_9 | 6.87e-20 | 67 | 301 | 1 | 242 | Glycosyltransferase family 9 (heptosyltransferase). Members of this family belong to glycosyltransferase family 9. Lipopolysaccharide is a major component of the outer leaflet of the outer membrane in Gram-negative bacteria. It is composed of three domains; lipid A, Core oligosaccharide and the O-antigen. All of these enzymes transfer heptose to the lipopolysaccharide core. |
PRK10422 | PRK10422 | 1.01e-10 | 1 | 269 | 8 | 291 | lipopolysaccharide core biosynthesis protein; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QCD43584.1 | 2.61e-142 | 1 | 328 | 6 | 333 |
QUB41015.1 | 7.76e-90 | 2 | 327 | 10 | 331 |
QRO15335.1 | 1.46e-82 | 2 | 329 | 5 | 343 |
QCY57932.1 | 1.46e-82 | 2 | 329 | 5 | 343 |
BBK92817.1 | 1.46e-82 | 2 | 329 | 5 | 343 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2GT1_A | 6.55e-06 | 2 | 281 | 4 | 293 | E.coli heptosyltransferase WaaC. [Escherichia coli UTI89],2GT1_B E. coli heptosyltransferase WaaC. [Escherichia coli UTI89] |
6DFE_A | 6.55e-06 | 2 | 281 | 4 | 293 | Thestructure of a ternary complex of E. coli WaaC [Escherichia coli],6DFE_B The structure of a ternary complex of E. coli WaaC [Escherichia coli] |
2H1F_A | 6.71e-06 | 2 | 281 | 4 | 293 | E.coli heptosyltransferase WaaC with ADP [Escherichia coli O6],2H1F_B E. coli heptosyltransferase WaaC with ADP [Escherichia coli O6],2H1H_A E. coli heptosyltransferase WaaC with ADP-2-deoxy-2-fluoro heptose [Escherichia coli RS218],2H1H_B E. coli heptosyltransferase WaaC with ADP-2-deoxy-2-fluoro heptose [Escherichia coli RS218] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9R9D5 | 2.48e-10 | 10 | 269 | 5 | 279 | Lipopolysaccharide core heptosyltransferase RfaQ OS=Escherichia coli OX=562 GN=rfaQ PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000040 | 0.000020 | 0.000004 | 0.000000 | 0.000000 | 0.000000 |
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