ID   LPXD_SYNSC              Reviewed;         347 AA.
AC   Q3AIH3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 87.
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=Syncc9605_1866;
OS   Synechococcus sp. (strain CC9605).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=110662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9605;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9605.";
RL   Submitted (JUL-2005) 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   -!- SEQUENCE CAUTION:
CC       Sequence=ABB35609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000110; ABB35609.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041435733.1; NC_007516.1.
DR   AlphaFoldDB; Q3AIH3; -.
DR   SMR; Q3AIH3; -.
DR   STRING; 110662.Syncc9605_1866; -.
DR   EnsemblBacteria; ABB35609; ABB35609; Syncc9605_1866.
DR   KEGG; syd:Syncc9605_1866; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_2_3; -.
DR   OrthoDB; 1602061at2; -.
DR   UniPathway; UPA00973; -.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProt.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0043886; F:structural constituent of carboxysome; IEA:UniProt.
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; 2.
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; Repeat; Transferase.
FT   CHAIN           1..347
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT                   /id="PRO_0000264443"
FT   ACT_SITE        248
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   347 AA;  35840 MW;  72B77C736C62214A CRC64;
     MRFSTLIKVL QTGDAGLRWS QAGLDPWLEG AASLDQASAA QLSFLEKGNA LTAALGASGV
     GALLLPDQQD LIDLASQRGI AFAVFADPRL AFAEALDQLY PRRRPLAEIH PSAVIDERAV
     VGPGTAVGPR VCIGEGSRLG ADCIVHPGVV IYDDVVVGDG CELHANAVLH PGSRLGRGCV
     VNSNAVVGSE GFGFVPTAKG WRKMPQTGQV VLEDGVEVGC GTTIDRPSVG ETRIGAGTKI
     DNLVQIGHGV TTGRGCAFAS QVGIAGGARI GHGVILAGQV GVANRAVVGD RAIASSKSGI
     HGDVAPGEVV SGFPAIPNRL WLRCANTFSK LPEMAKTLRE LKRDTPQ