ID   A3PCJ6_PROM0            Unreviewed;       344 AA.
AC   A3PCJ6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   02-SEP-2026, entry version 117.
DE   RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000256|HAMAP-Rule:MF_00523};
GN   Name=lpxD {ECO:0000256|HAMAP-Rule:MF_00523,
GN   ECO:0000313|EMBL:ABO17471.1};
GN   OrderedLocusNames=P9301_08481 {ECO:0000313|EMBL:ABO17471.1};
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO17471.1, ECO:0000313|Proteomes:UP000001430};
RN   [1] {ECO:0000313|EMBL:ABO17471.1, ECO:0000313|Proteomes:UP000001430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO17471.1,
RC   ECO:0000313|Proteomes:UP000001430};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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:0000256|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:0000256|HAMAP-Rule:MF_00523};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00523}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00523}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00523}.
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DR   EMBL; CP000576; ABO17471.1; -; Genomic_DNA.
DR   RefSeq; WP_011862822.1; NC_009091.1.
DR   AlphaFoldDB; A3PCJ6; -.
DR   STRING; 167546.P9301_08481; -.
DR   KEGG; pmg:P9301_08481; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_0_3; -.
DR   OrthoDB; 9784739at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001430; 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; 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; PF04613; LpxD; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_00523};
KW   Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW   Rule:MF_00523};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00523};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00523}; Reference proteome {ECO:0000313|Proteomes:UP000001430};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00523};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00523}.
FT   DOMAIN          25..97
FT                   /note="UDP-3-O-[3-hydroxymyristoyl] glucosamine N-
FT                   acyltransferase non-repeat region"
FT                   /evidence="ECO:0000259|Pfam:PF04613"
FT   DOMAIN          112..190
FT                   /note="Mannose-1-phosphate guanyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF25087"
FT   ACT_SITE        248
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   344 AA;  36980 MW;  BD49348B6CD7A659 CRC64;
     MLLSDLVDLI KKGNSNFISA NIFEDLNIDD AASLDAAVKH QISFLEENNI LKEKLDQTKA
     SAIITTNNDE IVSALKKLNI SNIIVKNPRI AFAEVLDYLY KTINFKPGIH ASAVIDKTAI
     IGADCHIGPN VYIGENTIIG DNNHILPGSS ILGNVQIGNN NIIHPNCVIY ENTTLKNNCV
     INSNSVIGSE GFGFIPENGK WVKMPQKGGV KIMSFVEIGT NCCIDRPAVG FTFIDEGTKL
     DNLIQIGHGV KIGKNCAFAA QVGIAGGANI GDGVILAGQV GVNNRVKVGN NVIASSKCGI
     HCDIEDGKVI SGFPAMENKS WLRSSSIFKK LPELAKKLRQ LDKQ
//