| Accession | TIGR01853 |
| Name | lipid_A_lpxD |
| Function | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD |
| Gene Symbol | lpxD |
| Trusted Cutoff | 242.50 |
| Domain Trusted Cutoff | 242.50 |
| Noise Cutoff | 112.45 |
| Domain Noise Cutoff | 112.45 |
| Isology Type | equivalog |
| EC Number | 2.3.1.191 |
| HMM Length | 325 |
| Mainrole Category | Cell envelope |
| Subrole Category | Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides |
| Gene Ontology Term | GO:0009245: lipid A biosynthetic process biological_process |
| | GO:0016410: N-acyltransferase activity molecular_function |
| Author | Haft DH |
| Entry Date | Mar 14 2003 11:03AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This HMM describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate). |
| References | DR URL; http://www.genome.ad.jp/dbget-bin/show_pathway?MAP00540+2.3.1.129
RN [1]
RM 10753930
RT Characterization of a novel lipid A containing D-galacturonic acid that replaces phosphate residues. The structure of the lipid A of the lipopolysaccharide from the hyperthermophilic bacterium Aquifex pyrophilus.
RA Plotz BM, Lindner B, Stetter KO, Holst O
RL J Biol Chem 2000 Apr 14;275(15):11222-8
DR HAMAP; MF_00523; 261 of 262 |
| Genome Property | GenProp0204: KDO(2)-lipid A (Re LPS) biosynthesis and delivery (HMM) |
