| Species | Alistipes timonensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes timonensis | |||||||||||
| CAZyme ID | MGYG000001562_02399 | |||||||||||
| CAZy Family | GT9 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 18814; End: 19800 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT9 | 57 | 299 | 6.5e-36 | 0.9688888888888889 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03789 | GT9_LPS_heptosyltransferase | 4.52e-42 | 1 | 318 | 10 | 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 | 1.34e-18 | 57 | 301 | 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. |
| PRK10964 | PRK10964 | 9.90e-06 | 168 | 287 | 189 | 299 | lipopolysaccharide heptosyltransferase RfaC. |
| PRK10422 | PRK10422 | 4.63e-05 | 189 | 262 | 216 | 291 | lipopolysaccharide core biosynthesis protein; Provisional |
| PRK10916 | PRK10916 | 5.95e-04 | 218 | 264 | 246 | 292 | ADP-heptose--LPS heptosyltransferase RfaF. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BBL09491.1 | 4.43e-182 | 1 | 320 | 1 | 320 |
| BBL01632.1 | 8.93e-182 | 1 | 320 | 1 | 320 |
| AFL77232.1 | 5.09e-181 | 1 | 320 | 20 | 339 |
| BBL07004.1 | 8.99e-175 | 1 | 320 | 1 | 320 |
| BBL13855.1 | 1.23e-153 | 1 | 321 | 13 | 332 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2GT1_A | 6.32e-08 | 157 | 286 | 178 | 298 | E.coli heptosyltransferase WaaC. [Escherichia coli UTI89],2GT1_B E. coli heptosyltransferase WaaC. [Escherichia coli UTI89] |
| 6DFE_A | 6.32e-08 | 157 | 286 | 178 | 298 | 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 | 6.51e-08 | 157 | 286 | 178 | 298 | 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 | 3.37e-07 | 157 | 286 | 178 | 298 | 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 |
|---|---|---|---|---|---|
| 1.000062 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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