ID   LPXD_TOLAT              Reviewed;         342 AA.
AC   C4L854;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=Tola_2101;
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001616; ACQ93700.1; -; Genomic_DNA.
DR   RefSeq; WP_015879168.1; NC_012691.1.
DR   AlphaFoldDB; C4L854; -.
DR   SMR; C4L854; -.
DR   STRING; 595494.Tola_2101; -.
DR   EnsemblBacteria; ACQ93700; ACQ93700; Tola_2101.
DR   KEGG; tau:Tola_2101; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_1_6; -.
DR   OMA; QIQIAHN; -.
DR   OrthoDB; 1602061at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000009073; 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.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
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_1000211755"
FT   ACT_SITE        238
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   342 AA;  36121 MW;  F7118B569D82F5B3 CRC64;
     MTITLGQLAQ HLGAELHGDA DVIIQRIANL ETAQAGEIGF LSDSKYQQYL ATTQASAVLL
     RAADLAMCQT NALVVKDPYI AFARVAQLLD STPAPAVNIH PSAVIADDVQ LGQGVAVGAN
     AVIETGVVLG DGAIIGAGCF VGKNSKLGAR SKLWANVTIY HNVRIGDDCL VQSGTVIGAD
     GFGYANERGE WIKIPQLGGV VIGNRVEIGS NTCIDRGAID DTRIADNVII DNLCQIAHNV
     EIGYGTAIAG AATFAGSTKI GKYCIIGGAS VFNGHIEICD QVTVTGMAMV MRSITEPGLY
     SSGIPAQTNK EWRKTAARTL HIDDMYKRLS NIEKLLDKQE QK