ID   LPXD_DESPS              Reviewed;         345 AA.
AC   Q6AJ06;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 97.
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}; OrderedLocusNames=DP2945;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG37674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR522870; CAG37674.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041278880.1; NC_006138.1.
DR   AlphaFoldDB; Q6AJ06; -.
DR   SMR; Q6AJ06; -.
DR   STRING; 177439.DP2945; -.
DR   EnsemblBacteria; CAG37674; CAG37674; DP2945.
DR   KEGG; dps:DP2945; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_0_7; -.
DR   OMA; VTIYDNC; -.
DR   OrthoDB; 1602061at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000602; 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; 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.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..345
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT                   /id="PRO_0000264364"
FT   ACT_SITE        241
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   345 AA;  35912 MW;  617AD2179F6FE66B CRC64;
     MKENITVAML AELVDGEVIG DGEVLVGNFV SLETAGEGDI TFLVKAGDQD LLTSTKAGAV
     IVHRKVEVES PATLIKVDDA YLAAAKIHTF LLEDEFSPEG IHRSAFVGEG CQISSEVTIK
     ALVSIGNRVV IGPRTRIESG VAIGDDVTIG EDCLLKANVT IADGSQLGNG VTIHSGTVIG
     SDGYGYATDK MGFHYKRPQV GTVRVDDNVE IGANSCVDRA TYGLTWIKSG AKIDNLVQIA
     HNVVVGENSL IVSQVGISGS TSLGRNVVMG GKAAAVGHLQ IGDGVMIAGG SGVLSNLSAG
     AVVGGIPARP IKQWRKSVVL TTKLPEMQKD IRALKKSVEE LAGKN