Species | Alistipes sp900541585 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900541585 | |||||||||||
CAZyme ID | MGYG000003279_00588 | |||||||||||
CAZy Family | GT9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 126228; End: 127358 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT9 | 103 | 345 | 3.5e-36 | 0.9688888888888889 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03789 | GT9_LPS_heptosyltransferase | 5.26e-45 | 38 | 362 | 1 | 275 | 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 | 6.22e-36 | 36 | 358 | 1 | 322 | ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis]. |
pfam01075 | Glyco_transf_9 | 8.24e-16 | 103 | 347 | 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 | 6.69e-07 | 38 | 333 | 2 | 299 | lipopolysaccharide heptosyltransferase RfaC. |
PRK10422 | PRK10422 | 1.34e-05 | 247 | 308 | 228 | 291 | lipopolysaccharide core biosynthesis protein; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AFL77232.1 | 3.65e-184 | 35 | 367 | 8 | 340 |
BBL09491.1 | 2.12e-176 | 47 | 367 | 1 | 321 |
BBL07004.1 | 2.86e-174 | 47 | 367 | 1 | 321 |
BBL01632.1 | 2.86e-174 | 47 | 367 | 1 | 321 |
BBL13855.1 | 2.36e-161 | 35 | 364 | 1 | 329 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2GT1_A | 4.71e-08 | 39 | 332 | 3 | 298 | E.coli heptosyltransferase WaaC. [Escherichia coli UTI89],2GT1_B E. coli heptosyltransferase WaaC. [Escherichia coli UTI89] |
6DFE_A | 4.71e-08 | 39 | 332 | 3 | 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 | 4.87e-08 | 39 | 332 | 3 | 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 | 4.45e-07 | 39 | 332 | 3 | 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 |
---|---|---|---|---|---|
1.000036 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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