| Species | Alistipes sp000434235 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp000434235 | |||||||||||
| CAZyme ID | MGYG000004006_01744 | |||||||||||
| CAZy Family | GT9 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 77586; End: 78623 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT9 | 80 | 322 | 6e-35 | 0.9644444444444444 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03789 | GT9_LPS_heptosyltransferase | 1.66e-40 | 14 | 341 | 1 | 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. |
| pfam01075 | Glyco_transf_9 | 3.94e-20 | 79 | 324 | 1 | 246 | 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 | 2.01e-05 | 203 | 285 | 206 | 291 | lipopolysaccharide core biosynthesis protein; Provisional |
| PRK10964 | PRK10964 | 2.21e-05 | 93 | 310 | 88 | 299 | lipopolysaccharide heptosyltransferase RfaC. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AFL77232.1 | 2.21e-177 | 12 | 344 | 9 | 340 |
| BBL07004.1 | 7.45e-176 | 23 | 345 | 1 | 322 |
| BBL01632.1 | 2.35e-165 | 23 | 344 | 1 | 321 |
| BBL09491.1 | 1.92e-164 | 23 | 345 | 1 | 322 |
| BBL13855.1 | 3.17e-151 | 12 | 341 | 2 | 329 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2GT1_A | 6.90e-09 | 15 | 295 | 3 | 291 | E.coli heptosyltransferase WaaC. [Escherichia coli UTI89],2GT1_B E. coli heptosyltransferase WaaC. [Escherichia coli UTI89] |
| 6DFE_A | 6.90e-09 | 15 | 295 | 3 | 291 | 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 | 7.15e-09 | 15 | 295 | 3 | 291 | 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 |
|---|---|---|---|---|---|---|
| P24173 | 1.52e-08 | 15 | 307 | 3 | 302 | Lipopolysaccharide heptosyltransferase 1 OS=Escherichia coli (strain K12) OX=83333 GN=rfaC PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000060 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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