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UDP-3-O-acylglucosamine N-acyltransferase (EC 2.3.1.-)

 LPXD_CHLTR              Reviewed;         354 AA.
P0CD76; O84245; Q9S530;
09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 1.
22-NOV-2017, entry version 50.
RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase;
EC=2.3.1.-;
Name=lpxD; OrderedLocusNames=CT_243;
Chlamydia trachomatis (strain D/UW-3/Cx).
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=272561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=D/UW-3/Cx;
PubMed=9784136; DOI=10.1126/science.282.5389.754;
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V.,
Davis R.W.;
"Genome sequence of an obligate intracellular pathogen of humans:
Chlamydia trachomatis.";
Science 282:754-759(1998).
[2]
IDENTIFICATION OF 3-HYDROXYARACHIDOYL-ACP AS PREDICTED SUBSTRATE, AND
FUNCTION.
STRAIN=L2;
PubMed=10358025; DOI=10.1074/jbc.274.24.16819;
Rund S., Lindner B., Brade H., Holst O.;
"Structural analysis of the lipopolysaccharide from Chlamydia
trachomatis serotype L2.";
J. Biol. Chem. 274:16819-16824(1999).
[3]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC AND
PALMITATE, ACTIVE SITE, AND SUBUNIT.
STRAIN=B;
PubMed=17360522; DOI=10.1073/pnas.0606356104;
Buetow L., Smith T.K., Dawson A., Fyffe S., Hunter W.N.;
"Structure and reactivity of LpxD, the N-acyltransferase of lipid A
biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 104:4321-4326(2007).
-!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-
myristoylglucosamine using 3-hydroxyarachidoyl-ACP as the acyl
donor. Is involved in the biosynthesis of lipid A, a
phosphorylated glycolipid that anchors the lipopolysaccharide to
the outer membrane of the cell (Probable).
{ECO:0000305|PubMed:10358025}.
-!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] +
UDP-3-O-acyl-alpha-D-glucosamine = UDP-2,3-diacyl-alpha-D-
glucosamine + [acyl-carrier-protein].
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
biosynthesis.
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17360522}.
-!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
LpxD subfamily. {ECO:0000305}.
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EMBL; AE001273; AAC67836.1; -; Genomic_DNA.
PIR; D71539; D71539.
RefSeq; NP_219748.1; NC_000117.1.
RefSeq; WP_009871590.1; NC_000117.1.
PDB; 2IU8; X-ray; 2.20 A; A/B/C=1-354.
PDB; 2IU9; X-ray; 3.10 A; A/B/C=1-354.
PDB; 2IUA; X-ray; 2.70 A; A/B/C=1-354.
PDBsum; 2IU8; -.
PDBsum; 2IU9; -.
PDBsum; 2IUA; -.
ProteinModelPortal; P0CD76; -.
SMR; P0CD76; -.
DIP; DIP-60889N; -.
EnsemblBacteria; AAC67836; AAC67836; CT_243.
GeneID; 884880; -.
KEGG; ctr:CT_243; -.
PATRIC; fig|272561.5.peg.260; -.
eggNOG; ENOG4105D7M; Bacteria.
eggNOG; COG1044; LUCA.
InParanoid; P0CD76; -.
KO; K02536; -.
OMA; GFGYAHT; -.
BRENDA; 2.3.1.191; 1315.
UniPathway; UPA00973; -.
EvolutionaryTrace; P0CD76; -.
Proteomes; UP000000431; Chromosome.
GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd03352; LbH_LpxD; 1.
HAMAP; MF_00523; LpxD; 1.
InterPro; IPR001451; Hexapep.
InterPro; IPR007691; LpxD.
InterPro; IPR011004; Trimer_LpxA-like_sf.
InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
PANTHER; PTHR43378; PTHR43378; 1.
Pfam; PF00132; Hexapep; 3.
Pfam; PF04613; LpxD; 1.
SUPFAM; SSF51161; SSF51161; 1.
TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Complete proteome;
Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
Reference proteome; Repeat; Transferase.
CHAIN 1 354 UDP-3-O-acylglucosamine N-
acyltransferase.
/FTId=PRO_0000059665.
REGION 190 192 UDP-GlcNAc binding.
ACT_SITE 247 247 Proton acceptor.
{ECO:0000305|PubMed:17360522}.
BINDING 240 240 Palmitate. {ECO:0000269|PubMed:17360522}.
BINDING 244 244 Palmitate. {ECO:0000269|PubMed:17360522}.
BINDING 248 248 UDP-GlcNAc.
{ECO:0000269|PubMed:17360522}.
BINDING 266 266 UDP-GlcNAc.
{ECO:0000269|PubMed:17360522}.
BINDING 284 284 UDP-GlcNAc.
{ECO:0000269|PubMed:17360522}.
SITE 43 43 Participates in a stacking interaction
with the uracil ring of UDP-GlcNAc.
SITE 49 49 Participates in a stacking interaction
with the uracil ring of UDP-GlcNAc.
HELIX 8 14 {ECO:0000244|PDB:2IU8}.
STRAND 18 21 {ECO:0000244|PDB:2IU8}.
TURN 33 35 {ECO:0000244|PDB:2IU8}.
STRAND 40 43 {ECO:0000244|PDB:2IU8}.
STRAND 46 48 {ECO:0000244|PDB:2IU8}.
HELIX 50 54 {ECO:0000244|PDB:2IU8}.
STRAND 59 64 {ECO:0000244|PDB:2IU8}.
HELIX 65 69 {ECO:0000244|PDB:2IU8}.
STRAND 78 83 {ECO:0000244|PDB:2IU8}.
HELIX 85 93 {ECO:0000244|PDB:2IU8}.
TURN 94 96 {ECO:0000244|PDB:2IU8}.
STRAND 117 119 {ECO:0000244|PDB:2IU9}.
STRAND 169 173 {ECO:0000244|PDB:2IU8}.
STRAND 184 188 {ECO:0000244|PDB:2IU8}.
STRAND 192 195 {ECO:0000244|PDB:2IU8}.
TURN 196 198 {ECO:0000244|PDB:2IU8}.
STRAND 199 202 {ECO:0000244|PDB:2IU8}.
STRAND 209 211 {ECO:0000244|PDB:2IU8}.
STRAND 222 225 {ECO:0000244|PDB:2IU8}.
STRAND 227 229 {ECO:0000244|PDB:2IU8}.
STRAND 231 233 {ECO:0000244|PDB:2IU8}.
STRAND 291 293 {ECO:0000244|PDB:2IU8}.
STRAND 307 310 {ECO:0000244|PDB:2IU8}.
TURN 311 314 {ECO:0000244|PDB:2IU8}.
HELIX 317 328 {ECO:0000244|PDB:2IU8}.
HELIX 330 342 {ECO:0000244|PDB:2IU8}.
SEQUENCE 354 AA; 38404 MW; B9C547C129AE17BB CRC64;
MSQSTYSLEQ LADFLKVEFQ GNGATLLSGV EEIEEAKTAH ITFLDNEKYA KHLKSSEAGA
IIISRTQFQK YRDLNKNFLI TSESPSLVFQ KCLELFITPV DSGFPGIHPT AVIHPTAIIE
DHVCIEPYAV VCQHAHVGSA CHIGSGSVIG AYSTVGEHSY IHPRVVIRER VSIGKRVIIQ
PGAVIGSCGF GYVTSAFGQH KHLKHLGKVI IEDDVEIGAN TTIDRGRFKH SVVREGSKID
NLVQIAHQVE VGQHSMIVAQ AGIAGSTKIG NHVIIGGQAG ITGHICIADH VIMMAQTGVT
KSITSPGIYG GAPARPYQEI HRQVAKVRNL PRLEERIAAL EKLVQKLEAL SEQH


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