ID   LPXD_BORA1              Reviewed;         361 AA.
AC   Q2L151;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
GN   Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523};
GN   OrderedLocusNames=BAV1744;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-
CC       hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of
CC       lipid A, a phosphorylated glycolipid that anchors the
CC       lipopolysaccharide to the outer membrane of the cell.
CC       {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + a (3R)-
CC         hydroxyacyl-[ACP] = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC         glucosamine + holo-[ACP] + H(+); 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   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000255|HAMAP-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; AM167904; CAJ49352.1; -; Genomic_DNA.
DR   RefSeq; WP_012417413.1; NC_010645.1.
DR   AlphaFoldDB; Q2L151; -.
DR   SMR; Q2L151; -.
DR   STRING; 360910.BAV1744; -.
DR   GeneID; 92935195; -.
DR   KEGG; bav:BAV1744; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_1_4; -.
DR   OrthoDB; 9784739at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001977; Chromosome.
DR   GO; GO:0103118; F:UDP-3-O-[(3R)-3-hydroxyacyl]-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   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 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   NCBIfam; TIGR01853; lipid_A_lpxD; 1.
DR   NCBIfam; NF002060; PRK00892.1; 1.
DR   PANTHER; PTHR43378; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR43378:SF2; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF04613; LpxD; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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..361
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT                   /id="PRO_0000264349"
FT   ACT_SITE        264
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   361 AA;  37027 MW;  98B55EBBD1A84CDE CRC64;
     MPVLLDSSRA PRLDALLSKG NTQGLECQID SPTGDLPLIA GIGTLASAGA QEIAFLSNPR
     YQSQVASTAA AAVIVTLDVA QALRAQGSTL VFVVCRHPYL LYARLAQWFD AERRGLPPAG
     VHPSAVVAPD AVIEEGASVG PQCVVDSGAR IGRGASLGPG CIVGQGSTVG ANSRLHARVT
     LYDGVHVGAR AIIHSGAVLG ADGFGFAPDP TLGKGAWGKI PQLGGVTVGN DVEIGANTTI
     DRGAIENTII GDGVKLDNLI MIAHNVRIGA HTAVAACVGI AGSTVIGERC IVGGAAMFSG
     HLSICDDVTI SGGTPVTSSI TKPGRYTGVY PYSEHGEWQR NAAVIQQLAL LRRRVRALEK
     A
//