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
61537
PubChem 445675
194791
23724479
1lxaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1j2zA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:SOG Unbound Unbound
1lxaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1j2zA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 125
1j2zA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121
1lxaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1j2zA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

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. Chemical modification and site-directed mutagenesis
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], [11] & [12], the reaction proceeds as follows:
(1) His125 (of 1lxa) acts as a general base, which activates the acceptor group, 3-OH of UDP-GlcNAc substrate, by abstracting a proton from the group.
(2) The activated hydroxyl group makes a nucleophilic attack on the transferred acyl group.

Created Updated
2003-11-07 2012-06-04