ID LPXB_SULSY Reviewed; 388 AA. AC B2V704; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 80. 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=SYO3AOP1_0140; OS Sulfurihydrogenibium sp. (strain YO3AOP1). OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=436114; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YO3AOP1; RX PubMed=19136599; DOI=10.1128/jb.01645-08; RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). 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; CP001080; ACD65786.1; -; Genomic_DNA. DR RefSeq; WP_012458876.1; NC_010730.1. DR AlphaFoldDB; B2V704; -. DR SMR; B2V704; -. DR STRING; 436114.SYO3AOP1_0140; -. DR CAZy; GT19; Glycosyltransferase Family 19. DR KEGG; sul:SYO3AOP1_0140; -. DR eggNOG; COG0763; Bacteria. DR HOGENOM; CLU_036577_3_1_0; -. DR UniPathway; UPA00973; -. 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..388 FT /note="Lipid-A-disaccharide synthase" FT /id="PRO_1000123067" SQ SEQUENCE 388 AA; 43452 MW; 1976F1C53872FAD3 CRC64; MKKIFLSVGE ISGDNYASEL AKHLKEYQIT GITGPKMRAI GVKPVANLED ISVVGLTEAL SKYKKIKEVF KQSVQALKSG VDLLIVVDFP GFNIKLLKEA KKLGIKTVYF ISPQVWAWGS GRVKEIVENT DLLISILPFE EEIYKPYVSD KFKFAYVGHP LLDIIKIYEN EDSFKQKLNI PKNKRIIGLL AGSRESEVNV ILPILIEAAR LLTKTFDDLH FVIPATVNMV DRVLEKVNFS LPITVITSNL SDKNLPKFEN PSYEVMKNAV FSIITSGTAT LEAAIIGNPF IIVYKVSPIT YFIGKKLVKI NYLGLPNIIA GNEIVPELLQ DRCNPLDIAN KTLEFLTDKN LYKTQKRNLE IVRKSLGKKG AIERASNLIR TLLEKGQA //