ID LPXB_COLP3 Reviewed; 393 AA. AC Q485F5; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 91. 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=CPS_1568; OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio OS psychroerythus). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=167879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=34H / ATCC BAA-681; RX PubMed=16043709; DOI=10.1073/pnas.0504766102; RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B., RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.; RT "The psychrophilic lifestyle as revealed by the genome sequence of RT Colwellia psychrerythraea 34H through genomic and proteomic analyses."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005). 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; CP000083; AAZ28777.1; -; Genomic_DNA. DR RefSeq; WP_011042404.1; NC_003910.7. DR AlphaFoldDB; Q485F5; -. DR SMR; Q485F5; -. DR STRING; 167879.CPS_1568; -. DR CAZy; GT19; Glycosyltransferase Family 19. DR KEGG; cps:CPS_1568; -. DR eggNOG; COG0763; Bacteria. DR HOGENOM; CLU_036577_3_0_6; -. DR UniPathway; UPA00973; -. DR Proteomes; UP000000547; Chromosome. 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1. 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..393 FT /note="Lipid-A-disaccharide synthase" FT /id="PRO_0000255175" SQ SEQUENCE 393 AA; 43815 MW; 380EDA95FF7BB4CC CRC64; MTTQNQNTHQ QTVFAMVVGE HSGDTLGAGL ITSLRQTHPH AKFIGIGGPK MLALGFESLF AMDELSVMGL VEVLGRIRRL LHVRKTLTDF FITNKPDVFI GIDAPDFNIG LELKLKVKGI KTVHYVSPSV WAWREKRIFK IAKATDMVLA LLPFEKAFYD KHNVPCTFVG HPLADDIPMQ SDKVLARDKL GLAQDKKILA LMPGSRGGEL SRLLEDFFES AKQLQAQDSE LLFVAPMISE QRANQFNALK AELAPDLDIE IVLNQTQQVM AASDCLLTAS GTVTLEAALI KRPMVICYKF SPITFFLGRR FVKLKWFSLP NLLTNKSLVP ELLQKDVCPE NIVPLVKERL YQDQSQLNDS FTAIHQQLKC DASKQAAKAV LDVLSSKLLS NNK //