ID   LPXD_CITBB              Reviewed;         345 AA.
AC   B5EEW8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Gbem_0841;
OS   Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS   Bem) (Geobacter bemidjiensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Citrifermentans.
OX   NCBI_TaxID=404380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter bemidjiensis BEM.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001124; ACH37864.1; -; Genomic_DNA.
DR   RefSeq; WP_012529275.1; NC_011146.1.
DR   AlphaFoldDB; B5EEW8; -.
DR   SMR; B5EEW8; -.
DR   STRING; 404380.Gbem_0841; -.
DR   EnsemblBacteria; ACH37864; ACH37864; Gbem_0841.
DR   KEGG; gbm:Gbem_0841; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_0_7; -.
DR   OMA; QIQIAHN; -.
DR   OrthoDB; 1602061at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000008825; 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; 2.
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_1000127680"
FT   ACT_SITE        237
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   345 AA;  35696 MW;  DFCEB1A419992BDD CRC64;
     MKKSLNEIAQ YLGGTVSGDG EVLIGGLATL DDAGEGTLTF LANPKYAAKV ATTKASAVLM
     GTGGNTHGKN AIFHPNPYLA FAKLLTLFYT APAKPVGVLP GAFVADGVKL GADVSVYPGA
     YIGAGAVIGD RVVLHPGVVL YPGVVVGNDV TLHANVSVRE RCRIGNRVTI HDGTVIGSDG
     FGYAPDGASY YKIPQIGIVI VEDDVEIGSN CVIDRAALEA TRIRRGTKID NLVQIAHNVV
     IGEDCIIVSQ VGISGSTQLG NHVTLGGQVG VAGHIKIGDN VMIGAKSGVA GNVEPNQVLS
     GIPVMPHRDW LRSAGIAPKL PEMKKTLSAL EKRVAELEAK LAKGE