LPXB_BURMA
ID LPXB_BURMA Reviewed; 388 AA.
AC Q62JD7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=BMA1542;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000010; AAU47742.1; -; Genomic_DNA.
DR RefSeq; WP_004192608.1; NC_006348.1.
DR RefSeq; YP_103182.1; NC_006348.1.
DR AlphaFoldDB; Q62JD7; -.
DR SMR; Q62JD7; -.
DR STRING; 243160.BMA1542; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; AAU47742; AAU47742; BMA1542.
DR GeneID; 56529046; -.
DR KEGG; bma:BMA1542; -.
DR PATRIC; fig|243160.12.peg.1586; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_4; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000006693; Chromosome 1.
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_0000255164"
SQ SEQUENCE 388 AA; 42012 MW; 56ACBF4FC1724EB5 CRC64;
MAFQLTPLRV ALVAGEPSGD LLGASLLGGL HARLPASSRY YGIGGPRMSA VEFDAHWPME
KLAVRGYVEA LKHIPEILRI RGELKRQLLA 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