ID   LPXD_PASMU              Reviewed;         342 AA.
AC   Q9CJL0; Q51923;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 114.
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}; Synonyms=firA;
GN   OrderedLocusNames=PM1994;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-339.
RC   STRAIN=9222;
RX   PubMed=7642134; DOI=10.1016/0378-1119(95)00254-4;
RA   Delamarche C., Manoha F., Behar G., Houlgatte R., Hellman U.,
RA   Wroblewski H.;
RT   "Characterization of the Pasteurella multocida skp and firA genes.";
RL   Gene 161:39-43(1995).
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 (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   -!- 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; AE004439; AAK04078.1; -; Genomic_DNA.
DR   EMBL; X74357; CAA52401.1; -; Genomic_DNA.
DR   PIR; S47342; S47342.
DR   RefSeq; WP_005725095.1; NC_002663.1.
DR   AlphaFoldDB; Q9CJL0; -.
DR   SMR; Q9CJL0; -.
DR   STRING; 747.DR93_2105; -.
DR   EnsemblBacteria; AAK04078; AAK04078; PM1994.
DR   KEGG; pmu:PM1994; -.
DR   HOGENOM; CLU_049865_0_1_6; -.
DR   OMA; QIQIAHN; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
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; 3.
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-acylglucosamine N-acyltransferase"
FT                   /id="PRO_0000059686"
FT   ACT_SITE        241
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   342 AA;  36049 MW;  117A01B0A04342D1 CRC64;
     MQVYSLQELA QQIGATIRGN ADVVVESIAP LDKATEKQLT FISNPKFRSL LAQSHAGILV
     VSEADVAFCA EQSNLLIVKD PYVAYAVLAQ YMDSTPKAAS GIAASAVVSA SAVIGKNVSI
     GANAVIEDGV TLGDHVVIGA NCFVGKNSKI GAYTQLWANV SVYHEVEIGQ HCLIQSGAVI
     GSDGFGYAND RGRWIKIPQV GQVIIGNHVE IGACTCIDRG ALDPTVIEDN VIIDNLCQIA
     HNVHIGTGTA VAGGVIMAGS LTVGRYCLIG GASVINGHME ICDKVTITGM GMVMRPITEP
     GVYSSGIPLQ TNKEWRKTAA LTLGIDAMNK RLKALEKKFE KK