LPXD_PHOLL
ID LPXD_PHOLL Reviewed; 342 AA.
AC Q7N8N7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
DE AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
GN Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; OrderedLocusNames=plu0682;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-
CC (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as
CC the acyl donor. Is involved in the biosynthesis of lipid A, a
CC phosphorylated glycolipid that anchors the lipopolysaccharide to the
CC outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-
CC alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78827, ChEBI:CHEBI:137740, ChEBI:CHEBI:137748;
CC EC=2.3.1.191; Evidence={ECO:0000255|HAMAP-Rule:MF_00523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-3-O-[(3R)-3-
CC hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + holo-[ACP] + UDP-
CC 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine;
CC Xref=Rhea:RHEA:17817, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:71573,
CC ChEBI:CHEBI:78474, ChEBI:CHEBI:78847; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00523};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 3/6. {ECO:0000255|HAMAP-
CC Rule:MF_00523}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}.
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DR EMBL; BX571861; CAE12977.1; -; Genomic_DNA.
DR RefSeq; WP_011145058.1; NC_005126.1.
DR AlphaFoldDB; Q7N8N7; -.
DR SMR; Q7N8N7; -.
DR STRING; 243265.plu0682; -.
DR EnsemblBacteria; CAE12977; CAE12977; plu0682.
DR GeneID; 24167969; -.
DR KEGG; plu:plu0682; -.
DR eggNOG; COG1044; Bacteria.
DR HOGENOM; CLU_049865_0_1_6; -.
DR OMA; QIQIAHN; -.
DR OrthoDB; 1602061at2; -.
DR BioCyc; PLUM243265:PLU_RS03375-MON; -.
DR UniPathway; UPA00359; UER00479.
DR Proteomes; UP000002514; Chromosome.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0103118; F:UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03352; LbH_LpxD; 1.
DR HAMAP; MF_00523; LpxD; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR007691; LpxD.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR PANTHER; PTHR43378; PTHR43378; 1.
DR Pfam; PF00132; Hexapep; 3.
DR Pfam; PF04613; LpxD; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Repeat; Transferase.
FT CHAIN 1..342
FT /note="UDP-3-O-(3-hydroxymyristoyl)glucosamine N-
FT acyltransferase"
FT /id="PRO_0000059687"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 342 AA; 36090 MW; AFE035678B64E029 CRC64;
MSSIRLADLA QQLNAQLHGD GDIVITSIAP MHSANGEQIT FLSDSRYRER LGECQAAAVV
LQASDLPYCN IPALVVANPY LAYAYMAQIM DTTPIPAQDI HSSAVISPQA TLGKNVAVGA
NAVIESGVVL GDNVVIGAGC FIGKNTRIGA GSRLWANVSV YHNVEMGEQC LIQSGAVIGS
DGFGYANDRG KWVKIPQLGS VIIGDRVEIG ACTTIDRGAL DNTIIGNGVI IDNQCQIAHN
VIIGDNTAVA GGVIMAGSLK IGCYCMIGGA SVINGHMEIC DKVTVTGMSM VMRPITEPGV
YSSGIPAQPN KVWRKTAALV MNINEMNKRL KSMESKLEDE NE
