Species | Duodenibacillus sp900544255 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Duodenibacillus; Duodenibacillus sp900544255 | |||||||||||
CAZyme ID | MGYG000003288_00784 | |||||||||||
CAZy Family | GT9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 10328; End: 11212 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT9 | 64 | 272 | 1.3e-28 | 0.8133333333333334 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam01075 | Glyco_transf_9 | 3.69e-29 | 61 | 274 | 16 | 228 | 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. |
COG0859 | RfaF | 1.53e-20 | 89 | 272 | 115 | 294 | ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis]. |
cd03789 | GT9_LPS_heptosyltransferase | 4.66e-18 | 124 | 274 | 95 | 241 | 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. |
PRK10422 | PRK10422 | 7.41e-10 | 136 | 290 | 160 | 325 | lipopolysaccharide core biosynthesis protein; Provisional |
PRK10964 | PRK10964 | 2.25e-07 | 172 | 260 | 190 | 284 | lipopolysaccharide heptosyltransferase RfaC. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDA55160.1 | 2.89e-136 | 1 | 294 | 17 | 311 |
QQS89241.1 | 2.17e-132 | 1 | 291 | 19 | 311 |
BBF22597.1 | 1.54e-131 | 1 | 285 | 18 | 303 |
ANU65198.1 | 8.54e-110 | 1 | 289 | 17 | 305 |
QQQ96353.1 | 8.54e-110 | 1 | 289 | 17 | 305 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2GT1_A | 5.16e-06 | 178 | 277 | 198 | 301 | E.coli heptosyltransferase WaaC. [Escherichia coli UTI89],2GT1_B E. coli heptosyltransferase WaaC. [Escherichia coli UTI89] |
6DFE_A | 5.16e-06 | 178 | 277 | 198 | 301 | 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 | 5.27e-06 | 178 | 277 | 198 | 301 | 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 |
---|---|---|---|---|---|---|
P45042 | 2.92e-06 | 62 | 273 | 84 | 305 | ADP-heptose--LPS heptosyltransferase 2 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=rfaF PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000059 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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