ID   LPXD_THEVB              Reviewed;         338 AA.
AC   Q8DMS9;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   02-SEP-2026, entry version 111.
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=tll0032;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Thermosynechococcaceae; Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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 UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + a (3R)-
CC         hydroxyacyl-[ACP] = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC         glucosamine + holo-[ACP] + H(+); 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; BA000039; BAC07585.1; -; Genomic_DNA.
DR   RefSeq; WP_011055887.1; NC_004113.1.
DR   AlphaFoldDB; Q8DMS9; -.
DR   SMR; Q8DMS9; -.
DR   STRING; 197221.gene:10746610; -.
DR   EnsemblBacteria; BAC07585; BAC07585; BAC07585.
DR   KEGG; tel:tll0032; -.
DR   PATRIC; fig|197221.4.peg.31; -.
DR   eggNOG; COG1044; Bacteria.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-ARBA.
DR   GO; GO:0043886; F:structural constituent of carboxysome shell; IEA:UniProtKB-ARBA.
DR   GO; GO:0103118; F:UDP-3-O-[(3R)-3-hydroxyacyl]-glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03352; LbH_LpxD; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR   HAMAP; MF_00523; LpxD; 1.
DR   InterPro; IPR056729; GMPPB_C.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR007691; LpxD.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR   NCBIfam; TIGR01853; lipid_A_lpxD; 1.
DR   NCBIfam; NF002060; PRK00892.1; 1.
DR   PANTHER; PTHR43378; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR43378:SF2; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF25087; GMPPB_C; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF04613; LpxD; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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..338
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT                   /id="PRO_0000059705"
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   338 AA;  35763 MW;  C45EA661C9DA45FF CRC64;
     MRLADVAERF GATLDCPEHG DRPVLGVAPL ETATATDISF LANPKYTALL QTTQAAAVFV
     RPDFQGEAAC PLLRVPHPYL AFAKCIEWFY PQPKPVAKIH PTAILGADVV LGAEVTIGAY
     TVIGDRVRIG DRTVIDSHCT LYDDVVIGSD CRIYSHCALR ERVQLGDRVI LQNSVVLGSD
     GFGYVPLPDG RHYKIPQVGT VVIGNDVEIG AGTTIDRATL GETTVANGTK IDNLTMVAHN
     CTIGENAILC AQVGLAGSTH IGNHVVLAGQ VGAAGHLTIG DRTVVSAKSG ISSSVPPDSR
     MGGIPAMDQT LYLKVSAAVK QLPDLLKRVR KLEAKVGE
//