ID   LPXB_RALN1              Reviewed;         390 AA.
AC   Q8XZH8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=RSc1417; ORFNames=RS05275;
OS   Ralstonia nicotianae (strain GMI1000) (Ralstonia solanacearum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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}.
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DR   EMBL; AL646052; CAD15119.1; -; Genomic_DNA.
DR   RefSeq; WP_011001366.1; NC_003295.1.
DR   AlphaFoldDB; Q8XZH8; -.
DR   SMR; Q8XZH8; -.
DR   STRING; 267608.RSc1417; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; CAD15119; CAD15119; RSc1417.
DR   GeneID; 60500940; -.
DR   KEGG; rso:RSc1417; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_4; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001436; 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; 2.
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..390
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190180"
SQ   SEQUENCE   390 AA;  42549 MW;  8AC1151064879FA9 CRC64;
     MTQPPAAPAR RIGMAAGEAS GDLLASLLLK GLHARLPRDV AYEGIGGARM AEQGFASHWP
     MHKLSVNGYV EVLGQLREIL AIRRELKQNL LADPPMAFIG VDAPDFNFNV EIAMRRAGVP
     VVHFVSPSIW AWRAGRIKTI ARAVDHILCL FPFEPEIYAR AGIPATYVGH PLADEIPLEP
     DVEGARSRLG LPLGRKVVAV LPGSRNSEVK LLGPTLFAAM ARMQAVEPDL AFVLPAANAM
     LRERIDAMRA EHPGLHLWVV DGQSHAAMEA ADVILLASGT ATLEAALYKK PMVITYKVPW
     LTAQIMKRKG YLPYVGLPNI LSGRFVVPEL LQDDATPEAL ARETLLQLSD HANAAFLREH
     FTQMHLTLKQ NMADIGAQVV VDLLRGRGKL
//