Species | Alistipes sp900544265 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900544265 | |||||||||||
CAZyme ID | MGYG000002082_01649 | |||||||||||
CAZy Family | GT9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 79839; End: 80873 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT9 | 76 | 318 | 1.7e-36 | 0.9688888888888889 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03789 | GT9_LPS_heptosyltransferase | 1.88e-40 | 11 | 337 | 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. |
COG0859 | RfaF | 1.24e-36 | 9 | 343 | 1 | 334 | ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis]. |
pfam01075 | Glyco_transf_9 | 1.84e-17 | 76 | 320 | 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 | 9.14e-07 | 219 | 281 | 227 | 291 | lipopolysaccharide core biosynthesis protein; Provisional |
PRK10964 | PRK10964 | 5.34e-05 | 193 | 340 | 195 | 321 | lipopolysaccharide heptosyltransferase RfaC. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AFL77232.1 | 1.05e-177 | 1 | 341 | 1 | 341 |
BBL07004.1 | 2.27e-172 | 20 | 341 | 1 | 322 |
BBL01632.1 | 3.05e-163 | 20 | 341 | 1 | 322 |
BBL09491.1 | 6.14e-163 | 20 | 339 | 1 | 320 |
BBL13855.1 | 1.54e-158 | 8 | 340 | 1 | 332 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2GT1_A | 3.00e-06 | 13 | 291 | 4 | 291 | E.coli heptosyltransferase WaaC. [Escherichia coli UTI89],2GT1_B E. coli heptosyltransferase WaaC. [Escherichia coli UTI89] |
6DFE_A | 3.00e-06 | 13 | 291 | 4 | 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 | 3.07e-06 | 13 | 291 | 4 | 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 | 6.74e-06 | 13 | 299 | 4 | 306 | 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 |
---|---|---|---|---|---|
1.000043 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.