CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.160 | 3 Solenoid |
|
2.160.10 | UDP N-Acetylglucosamine Acyltransferase; domain 1 |
|
2.160.10.10 | Hexapeptide repeat proteins |
Domain Context
CATH Clusters
| Superfamily | Hexapeptide repeat proteins |
| Functional Family | UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase |
Enzyme Information
| 2.3.1.191 |
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase.
based on mapping to UniProt P21645
(3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-3-O-((3R)- hydroxytetradecanoyl)-alpha-D-glucosamine = UDP-2-N,3-O-bis((3R)-3- hydroxytetradecanoyl)-alpha-D-glucosamine + a holo-[acyl-carrier- protein].
-!- The enzyme catalyzes a step of lipid A biosynthesis. -!- LpxD from Escherichia coli prefers (R,S)-3-hydroxymyristoyl-[acyl- carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein]. -!- E.coli lipid A acyltransferases do not have an absolute specificity for 14-carbon hydroxy fatty acids but can transfer fatty acids differing by one carbon unit if the fatty acid substrates are available. -!- When grown on 1% propionic acid, lipid A also contains the odd-chain fatty acids tridecanoic acid, pentadecanoic acid, hydroxytridecanoic acid, and hydroxypentadecanoic acid. -!- Formerly EC 2.3.1.n1.
|
UniProtKB Entries (1)
| P21645 |
LPXD_ECOLI
Escherichia coli K-12
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
|
PDB Structure
| PDB | 3EH0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis
Biochemistry
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