ID   LPXB_BURP1              Reviewed;         388 AA.
AC   Q3JR42;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=BURPS1710b_2569;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
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; CP000124; ABA47758.1; -; Genomic_DNA.
DR   RefSeq; WP_004527287.1; NC_007434.1.
DR   AlphaFoldDB; Q3JR42; -.
DR   SMR; Q3JR42; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ABA47758; ABA47758; BURPS1710b_2569.
DR   KEGG; bpm:BURPS1710b_2569; -.
DR   HOGENOM; CLU_036577_3_0_4; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002700; 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   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_0000255166"
SQ   SEQUENCE   388 AA;  42030 MW;  03FD6484CAC24EC5 CRC64;
     MAFQLTPLRV ALVAGEPSGD LLGASLLGGL HARLPASSRY YGIGGPRMSA VEFDAHWPME
     KLAVRGYVEA LKHIPEILRI RGELKRQLLA EPPDAFVGID APDFNFGLEP ALRGAGIPTI
     HFVCPSIWAW RGGRIKKIVK AVDHMLCLFP FEPELLEKAG VAATFVGHPL ADEIPLEPDT
     HGARIALGLP GGGPVIAVLP GSRRSEIELI GPTFFDAMEL MQQREPGVRF VVPAATPALR
     ALLQPLVDAH PSLSVTLTEG RAQVAMTAAD AILVKSGTVT LEAALLKKPM VISYKVPWLT
     GQIMRRQGYL PYVGLPNILA GRFVVPELLQ HFATPDALAD ATLTQLRDDA NRRALTDIFT
     DMHLALRQNT AQRAAEAVAR VIDSRKPR
//