ID   LPXD3_GLOVI             Reviewed;         345 AA.
AC   Q7NH24;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase 3 {ECO:0000255|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
GN   Name=lpxD3 {ECO:0000255|HAMAP-Rule:MF_00523}; OrderedLocusNames=glr2713;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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; BA000045; BAC90654.1; -; Genomic_DNA.
DR   RefSeq; NP_925659.1; NC_005125.1.
DR   RefSeq; WP_011142707.1; NC_005125.1.
DR   AlphaFoldDB; Q7NH24; -.
DR   SMR; Q7NH24; -.
DR   STRING; 251221.35213282; -.
DR   PRIDE; Q7NH24; -.
DR   EnsemblBacteria; BAC90654; BAC90654; BAC90654.
DR   KEGG; gvi:glr2713; -.
DR   PATRIC; fig|251221.4.peg.2740; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_0_3; -.
DR   InParanoid; Q7NH24; -.
DR   OMA; QIQIAHN; -.
DR   OrthoDB; 1602061at2; -.
DR   PhylomeDB; Q7NH24; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000557; Chromosome.
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; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..345
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase 3"
FT                   /id="PRO_0000059675"
FT   ACT_SITE        236
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   345 AA;  36898 MW;  26CE288804507A74 CRC64;
     MKLGELAAHL GCPVEGNPDV EIRGLASIQQ AGPGELSFIE SEKYARFIKL TRAEALILDW
     RTPVSKVPCI RSEQPRLTFA HALELFYQPR RPAPGIHPTA ILGANVQLGE NVHLGAYVVI
     GDDVTIGPEA VIYPNCTIYN DVRIGVRTVV HANCVLHERT KIGDECIVQS GAVVGGEGFG
     FVPTPEGTWH KMPQSGYVRV EDQVEIGSNA AIDRPSVGFT HIGRGTKIDN LVMVGHGCEI
     GEHCLLVGQV GLAGGVKLGR NVVLAGQVGV AGHAAIGDRT VVSAQSGIPS DVEPGTVVSG
     SPALPHALWL RTSALIRRLP ELFQNLRDLQ RKVALLQQRL DSGHH