LPXB_BURP1
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 03-AUG-2022, entry version 76.
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; Proteobacteria; 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 OMA; PTVWAWR; -.
DR OrthoDB; 1258510at2; -.
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 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_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
