ID   LPXD_AGRFC              Reviewed;         355 AA.
AC   Q8UFL5;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=Atu1382;
GN   ORFNames=AGR_C_2556;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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; AE007869; AAK87174.1; -; Genomic_DNA.
DR   PIR; AF2746; AF2746.
DR   PIR; E97527; E97527.
DR   RefSeq; NP_354389.1; NC_003062.2.
DR   RefSeq; WP_010971576.1; NC_003062.2.
DR   AlphaFoldDB; Q8UFL5; -.
DR   SMR; Q8UFL5; -.
DR   STRING; 176299.Atu1382; -.
DR   EnsemblBacteria; AAK87174; AAK87174; Atu1382.
DR   KEGG; atu:Atu1382; -.
DR   PATRIC; fig|176299.10.peg.1405; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_2_5; -.
DR   OMA; QIQIAHN; -.
DR   PhylomeDB; Q8UFL5; -.
DR   BioCyc; AGRO:ATU1382-MON; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000813; Chromosome circular.
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; IPR018357; Hexapep_transf_CS.
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; 3.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..355
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT                   /id="PRO_0000059641"
FT   ACT_SITE        258
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   355 AA;  36885 MW;  5BA1926786D9DE93 CRC64;
     MEYNAFFPPH EGLRLKDIAD LFGAELSDDA AGERIIRSVA PVYRAKPDQL CYILSRKSGE
     ELLTCEAGAV ICDAALKSLI PSHIPALISK TPHTLFAQVG ALLHPSAMRP SLVARMEAEI
     SPAAYVDPSA KLEPGVIVEP MAVIGAGVHI GAGTRIGPGV VIGSDVQIGR DCTIAGGASI
     LAALLGNNVI IHNGARIGQD GFGYAPGPRG MLKIVQIGRV IIQDHVEVGA NTTIDRGTMD
     DTVIGEGTKI DNQVQIGHNV RIGRHCGIVS GVGIAGSTRI GDGVMIGGAT GVNGHITIGD
     GVQIAAMSGV VSDVPAGTRY GGIPARPMKH FLRDMADILA RAEERDKKTG EKNNG