ID LPXB_BURL3 Reviewed; 389 AA. AC Q39F56; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392}; DE EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392}; GN Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392}; GN OrderedLocusNames=Bcep18194_A5316; OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / OS R18194 / 383). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=482957; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia sp. 383."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3- CC diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor CC of lipid A, a phosphorylated glycolipid that anchors the CC lipopolysaccharide to the outer membrane of the cell. CC {ECO:0000255|HAMAP-Rule:MF_00392}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D- CC glucosamine = a lipid A disaccharide + H(+) + UDP; CC Xref=Rhea:RHEA:67828, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:137748, ChEBI:CHEBI:176338, ChEBI:CHEBI:176343; CC EC=2.4.1.182; Evidence={ECO:0000255|HAMAP-Rule:MF_00392}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00392}. CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP- CC Rule:MF_00392}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000151; ABB08910.1; -; Genomic_DNA. DR RefSeq; WP_011352448.1; NZ_WNDV01000025.1. DR AlphaFoldDB; Q39F56; -. DR SMR; Q39F56; -. DR CAZy; GT19; Glycosyltransferase Family 19. DR GeneID; 45095192; -. DR KEGG; bur:Bcep18194_A5316; -. DR PATRIC; fig|482957.22.peg.2265; -. DR HOGENOM; CLU_036577_3_0_4; -. DR UniPathway; UPA00973; -. DR Proteomes; UP000002705; Chromosome 1. DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_00392; LpxB; 1. DR InterPro; IPR003835; Glyco_trans_19. DR NCBIfam; TIGR00215; lpxB; 1. DR PANTHER; PTHR30372; LIPID-A-DISACCHARIDE SYNTHASE; 1. DR PANTHER; PTHR30372:SF7; LIPID-A-DISACCHARIDE SYNTHASE; 1. DR Pfam; PF02684; LpxB; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis; KW Lipid metabolism; Transferase. FT CHAIN 1..389 FT /note="Lipid-A-disaccharide synthase" FT /id="PRO_0000255167" SQ SEQUENCE 389 AA; 42301 MW; 8DE9374492AC2D54 CRC64; MPLPTSQLRL AMVAGEPSGD LLGASLLGGL RERLPESAQY YGIGGQRMIA QGFDSHWQMD KLTVRGYVEA LGQIPEILRI RGELKRQLLA ERPDAFIGVD APDFNFNVEQ AARDAGIPSI HFVCPSIWAW RGGRIKKIAK SVDHMLCLFP FEPAILDKAG VASTYVGHPL ADEIPLEPDT HGARIALGLP ADGPVIAVLP GSRRSEIALI GPTFFAAMAL MQQREPGVRF VMPAATPALR ALLQPLVDAH PKLALTITDG RSQVAMTAAD AILVKSGTVT LEAALLKKPM VISYKVPWLT GQIMRRQGYL PYVGLPNILA GRFVVPELLQ HFATPEALAD ATLTQLRDDA NRRTLTEIFT EMHLSLRQNT AAKAAEAVVR VLEQRKGRA //