LPXD_CUPMC
ID LPXD_CUPMC Reviewed; 369 AA.
AC Q1LNE8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Rmet_1445;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF08328.1; -; Genomic_DNA.
DR RefSeq; WP_011516195.1; NC_007973.1.
DR AlphaFoldDB; Q1LNE8; -.
DR SMR; Q1LNE8; -.
DR STRING; 266264.Rmet_1445; -.
DR EnsemblBacteria; ABF08328; ABF08328; Rmet_1445.
DR KEGG; rme:Rmet_1445; -.
DR eggNOG; COG1044; Bacteria.
DR HOGENOM; CLU_049865_0_1_4; -.
DR OMA; QIQIAHN; -.
DR OrthoDB; 1602061at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000002429; Chromosome.
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; 2.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Repeat; Transferase.
FT CHAIN 1..369
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_0000264420"
FT REGION 348..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 369 AA; 38502 MW; 51F22128C5CA3979 CRC64;
MKTPTLGQLA TENGAQVVGD PDLAVVGLAP LDQAGPGDLS FLSNPLYLPQ ALASAAGAVI
VSPADLERIR ADGQAEGRNW LVARNPYVCF ARVAQRFDRA ANADSRTGID PRASVAPDAV
VPASCFIGPN VVIESGARLG ERVRILANAF IGASAEIGED TLIYANVSVY HRCVIGARNI
LHSGAVIGAD GFGFAPDIGP TGVEYVKIPQ VGRAVLGNDV EIGANTAVDR GAMADTVIED
GCKIDNQVQI AHNVHVGAHT VIAGTAAVSG STKIGRFCVI GGAANFSGHL NIADRTTVSG
GTSITKSITK PGGHYTSVFP FTSHGEWERN AAIVRGLSKL RERVVQLERR QRGENNAPAQ
NKQDEEKSS