ID   LPXB_BURM9              Reviewed;         388 AA.
AC   A2SB86;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=BMA10229_A3269;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000546; ABN02969.1; -; Genomic_DNA.
DR   RefSeq; WP_004266728.1; NC_008836.1.
DR   AlphaFoldDB; A2SB86; -.
DR   SMR; A2SB86; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ABN02969; ABN02969; BMA10229_A3269.
DR   GeneID; 56595931; -.
DR   KEGG; bml:BMA10229_A3269; -.
DR   HOGENOM; CLU_036577_3_0_4; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002283; Chromosome I.
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   PANTHER; PTHR30372; PTHR30372; 1.
DR   Pfam; PF02684; LpxB; 1.
DR   TIGRFAMs; TIGR00215; lpxB; 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_1000049388"
SQ   SEQUENCE   388 AA;  42046 MW;  97C10E27E3D0C6BA CRC64;
     MAFQLTPLRV ALVAGEPSGD LLGASLLGGL HARLPASSRY YGIGGPRMSA VEFDAHWPME
     KLAVRGYVEA LKHIPEILRI RGELKRQLFA EPPDAFVGID APDFNFGLEQ ALRGAGIPTI
     HFVCPSIWAW RGGRIKKIVK AVDHMLCLFP FEPELLEKAG VAATFVGHPL ADEIPLEPDT
     HGARIALGLP GGGPVIAVLP GSRRSEIELI GPTFFDAMEL MQQREPGVRF VVPAATPALR
     ALLQPLVDAH PSLSVTLTEG RAQVAMTAAD AILVKSGTVT LEAALLKKPM VISYKVPWLT
     GQIMRRQGYL PYVGLPNILA GRFVVPELLQ HFATPDALAD ATLTQLRDDA NRRALADIFT
     DMHLALRQNT AQRAAEAVAH VIDSRKPR