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LPXB_ENT38
ID   LPXB_ENT38              Reviewed;         382 AA.
AC   A4W6S7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=Ent638_0720;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(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=2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl
CC         1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC         glucosamine = H(+) + lipid A disaccharide (E. coli) + UDP;
CC         Xref=Rhea:RHEA:22668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57957,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58466, ChEBI:CHEBI:78847;
CC         Evidence={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: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC       from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC       acetyl-alpha-D-glucosamine: step 5/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00392}.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00392}.
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DR   EMBL; CP000653; ABP59407.1; -; Genomic_DNA.
DR   RefSeq; WP_012016128.1; NC_009436.1.
DR   AlphaFoldDB; A4W6S7; -.
DR   SMR; A4W6S7; -.
DR   STRING; 399742.Ent638_0720; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ABP59407; ABP59407; Ent638_0720.
DR   KEGG; ent:Ent638_0720; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00359; UER00481.
DR   Proteomes; UP000000230; 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   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..382
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000060771"
SQ   SEQUENCE   382 AA;  42414 MW;  F58C239A9246CA78 CRC64;
     MVDNRPLTIA LVAGETSGDI LGAGLIRALK AREPNARFVG VAGPLMQAEG CEAWYEMEEL
     AVMGIVEVLG RLRRLLHIRA DLTGRFTDLK PDVFVGIDAP DFNITLEGNL KKQGIKTIHY
     VSPSVWAWRQ KRVFKIGRST DMVLAFLPFE KAFYDRFNVP CRFIGHTMAD AMPLDPDKNA
     ARDSLGIPHD AHCLALLPGS RGAEVEMLSA DFLRTAQILR QTYPDLEVVV PLVNAKRREQ
     FERIKAAVAP DLHIHLLDGK GREAMVASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF
     WLAKRLVKTD YVSLPNLLAG RELVKELLQD ECQPQALADA LLPLLADGKT RHQMHDTFRE
     LHQQIRCNAD EQAADAVMEL AQ
 
 
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