You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000002507_01613
You are here: Home > Sequence: MGYG000002507_01613
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Escherichia albertii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia; Escherichia albertii | |||||||||||
| CAZyme ID | MGYG000002507_01613 | |||||||||||
| CAZy Family | GT9 | |||||||||||
| CAZyme Description | Lipopolysaccharide core heptosyltransferase RfaQ | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 111604; End: 112674 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK10422 | PRK10422 | 0.0 | 1 | 352 | 1 | 352 | lipopolysaccharide core biosynthesis protein; Provisional |
| TIGR02201 | heptsyl_trn_III | 1.18e-174 | 7 | 344 | 1 | 344 | lipopolysaccharide heptosyltransferase III, putative. This family consists of examples of the putative ADP-heptose:LPS heptosyltransferase III, an enzyme of LPS inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria. This enzyme may be less widely distributed than heptosyltransferases I and II. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] |
| pfam01075 | Glyco_transf_9 | 1.10e-101 | 77 | 327 | 2 | 247 | 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 | 3.85e-96 | 6 | 346 | 2 | 333 | ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis]. |
| cd03789 | GT9_LPS_heptosyltransferase | 4.27e-62 | 7 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QKD63499.1 | 4.54e-266 | 1 | 356 | 1 | 356 |
| QCZ30476.1 | 1.85e-265 | 1 | 356 | 1 | 356 |
| QLM98344.1 | 7.53e-265 | 1 | 356 | 1 | 356 |
| VED16238.1 | 3.07e-264 | 1 | 356 | 1 | 356 |
| AQV35048.1 | 3.07e-264 | 1 | 356 | 1 | 356 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3TOV_A | 2.34e-24 | 2 | 345 | 5 | 347 | Thecrystal structure of the glycosyl transferase family 9 from Veillonella parvula DSM 2008 [Veillonella parvula DSM 2008],3TOV_B The crystal structure of the glycosyl transferase family 9 from Veillonella parvula DSM 2008 [Veillonella parvula DSM 2008] |
| 2GT1_A | 4.26e-07 | 7 | 292 | 2 | 283 | E.coli heptosyltransferase WaaC. [Escherichia coli UTI89],2GT1_B E. coli heptosyltransferase WaaC. [Escherichia coli UTI89] |
| 6DFE_A | 4.26e-07 | 7 | 292 | 2 | 283 | 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 | 4.38e-07 | 7 | 292 | 2 | 283 | 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] |
| 1PSW_A | 8.15e-07 | 7 | 298 | 2 | 297 | Structureof E. coli ADP-heptose lps heptosyltransferase II [Escherichia coli] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P25742 | 8.70e-253 | 13 | 356 | 1 | 344 | Lipopolysaccharide core heptosyltransferase RfaQ OS=Escherichia coli (strain K12) OX=83333 GN=rfaQ PE=3 SV=2 |
| Q9R9D5 | 3.41e-180 | 13 | 344 | 1 | 332 | Lipopolysaccharide core heptosyltransferase RfaQ OS=Escherichia coli OX=562 GN=rfaQ PE=1 SV=1 |
| P45042 | 1.35e-09 | 8 | 301 | 3 | 300 | ADP-heptose--LPS heptosyltransferase 2 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=rfaF PE=3 SV=1 |
| P37692 | 5.93e-08 | 7 | 298 | 2 | 297 | ADP-heptose--LPS heptosyltransferase 2 OS=Escherichia coli (strain K12) OX=83333 GN=rfaF PE=1 SV=1 |
| P37421 | 1.41e-07 | 7 | 298 | 2 | 297 | ADP-heptose--LPS heptosyltransferase 2 OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=rfaF PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000050 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |