DB code: D00464
| RLCP classification | 3.1107.6300.74 : Transfer | |
|---|---|---|
| CATH domain | 2.160.10.10 : UDP N-Acetylglucosamine Acyltransferase; domain 1 | Catalytic domain |
| 1.20.1180.10 : Udp N-acetylglucosamine O-acyltransferase; Domain 2 | ||
| E.C. | 2.3.1.129 | |
| CSA | 1lxa | |
| M-CSA | 1lxa | |
| MACiE | M0069 | |
| CATH domain | Related DB codes (homologues) |
|---|---|
| 2.160.10.10 : UDP N-Acetylglucosamine Acyltransferase; domain 1 | S00167 D00094 D00417 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0A722 |
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
|
UDP-N-acetylglucosamine acyltransferase
EC 2.3.1.129 |
NP_414723.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_488483.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF00132
(Hexapep)
[Graphical View] |
| O25927 |
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
|
UDP-N-acetylglucosamine acyltransferase
EC 2.3.1.129 |
NP_208166.1
(Protein)
NC_000915.1 (DNA/RNA sequence) YP_006935297.1 (Protein) NC_018939.1 (DNA/RNA sequence) |
PF00132
(Hexapep)
[Graphical View] |
| KEGG enzyme name |
|---|
|
acyl-[acyl-carrier-protein]---UDP-N-acetylglucosamineO-acyltransferase
UDP-N-acetylglucosamine acyltransferase uridine diphosphoacetylglucosamine acyltransferase acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamineO-acyltransferase (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0A722 | LPXA_ECOLI | (R)-3-hydroxytetradecanoyl-[acyl-carrier- protein] + UDP-N-acetylglucosamine = [acyl-carrier-protein] + UDP- 3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine. | Homotrimer. | Cytoplasm. | |
| O25927 | LPXA_HELPY | (R)-3-hydroxytetradecanoyl-[acyl-carrier- protein] + UDP-N-acetylglucosamine = [acyl-carrier-protein] + UDP- 3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine. | Homotrimer (By similarity). | Cytoplasm (By similarity). |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00540 | Lipopolysaccharide biosynthesis |
| Compound table | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | ||||||||
| KEGG-id | C04688 | C00043 | C00229 | C04738 | ||||||
| E.C. | ||||||||||
| Compound | (R)-3-Hydroxytetradecanoyl-[acyl-carrier protein] | UDP-N-acetylglucosamine | Acyl-carrier protein | UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine | ||||||
| Type | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | amide group,carbohydrate,nucleotide | carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfhydryl group | amide group,carbohydrate,lipid,nucleotide | ||||||
| ChEBI |
16264 16264 |
61537 61537 |
||||||||
| PubChem |
445675 445675 |
194791 23724479 194791 23724479 |
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| 1lxaA01 |
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Unbound | Unbound | Unbound | Unbound | |
| 1j2zA01 |
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Unbound | Analogue:SOG | Unbound | Unbound | |
| 1lxaA02 |
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Unbound | Unbound | Unbound | Unbound | |
| 1j2zA02 |
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Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| literature [8] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1lxaA01 |
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HIS 125 | ||||
| 1j2zA01 |
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HIS 121 | ||||
| 1lxaA02 |
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| 1j2zA02 |
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| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[8]
|
FIG. 6, p.27054 | |
|
[11]
|
p.774 | |
|
[12]
|
p.1385-1386 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2180947 |
| Journal | J Biol Chem |
| Year | 1990 |
| Volume | 265 |
| Pages | 6394-402 |
| Authors | Galloway SM, Raetz CR |
| Title | A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8293817 |
| Journal | FEBS Lett |
| Year | 1994 |
| Volume | 337 |
| Pages | 289-92 |
| Authors | Vuorio R, Harkonen T, Tolvanen M, Vaara M |
| Title | The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of lipid A biosynthesis is conserved in various bacteria. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7567967 |
| Journal | Proteins |
| Year | 1995 |
| Volume | 22 |
| Pages | 191-2 |
| Authors | Pfitzner U, Raetz CR, Roderick SL |
| Title | Crystallization of UDP-N-acetylglucosamine O-acyltransferase from Escherichia coli |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). |
| Medline ID | 96069822 |
| PubMed ID | 7481807 |
| Journal | Science |
| Year | 1995 |
| Volume | 270 |
| Pages | 997-1000 |
| Authors | Raetz CR, Roderick SL |
| Title | A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase |
| Related PDB | 1lxa |
| Related UniProtKB | P0A722 |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9242624 |
| Journal | J Biol Chem |
| Year | 1997 |
| Volume | 272 |
| Pages | 19688-96 |
| Authors | Odegaard TJ, Kaltashov IA, Cotter RJ, Steeghs L, van der Ley P, Khan S, Maskell DJ, Raetz CR |
| Title | Shortened hydroxyacyl chains on lipid A of Escherichia coli cells expressing a foreign UDP-N-acetylglucosamine O-acyltransferase |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9829962 |
| Journal | J Biol Chem |
| Year | 1998 |
| Volume | 273 |
| Pages | 32369-72 |
| Authors | Wyckoff TJ, Lin S, Cotter RJ, Dotson GD, Raetz CR |
| Title | Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9575543 |
| Journal | Prog Clin Biol Res |
| Year | 1998 |
| Volume | 397 |
| Pages | 1-14 |
| Authors | Raetz CR |
| Title | Enzymes of lipid A biosynthesis |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10480918 |
| Journal | J Biol Chem |
| Year | 1999 |
| Volume | 274 |
| Pages | 27047-55 |
| Authors | Wyckoff TJ, Raetz CR |
| Title |
The active site of Escherichia coli UDP-N-acetylglucosamine acyltransferase. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10653812 |
| Journal | Biophys J |
| Year | 2000 |
| Volume | 78 |
| Pages | 994-1000 |
| Authors | Khurana R, Fink AL |
| Title | Do parallel beta-helix proteins have a unique fourier transform infrared spectrum? |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11976505 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 2002 |
| Volume | 58 |
| Pages | 864-6 |
| Authors | Lee BI, Lee JY, Moon J, Han BW, Suh SW |
| Title | Crystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine acyltransferase from Helicobacter pylori. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14579368 |
| Journal | Proteins |
| Year | 2003 |
| Volume | 53 |
| Pages | 772-4 |
| Authors | Lee BI, Suh SW |
| Title | Crystal structure of UDP-N-acetylglucosamine acyltransferase from Helicobacter pylori. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15491619 |
| Journal | J Mol Biol |
| Year | 2004 |
| Volume | 343 |
| Pages | 1379-89 |
| Authors | Jain NU, Wyckoff TJ, Raetz CR, Prestegard JH |
| Title | Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
According to the literature [8], (1) His125 (of 1lxa) acts as a general base, (2) The activated hydroxyl group makes a nucleophilic attack on the transferred acyl group. |
| Created | Updated |
|---|---|
| 2003-11-07 | 2012-06-04 |