ID   LPXB_PSEPG              Reviewed;         375 AA.
AC   B0KSB2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
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=PputGB1_1159;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000926; ABY97067.1; -; Genomic_DNA.
DR   RefSeq; WP_012270846.1; NC_010322.1.
DR   AlphaFoldDB; B0KSB2; -.
DR   SMR; B0KSB2; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; ppg:PputGB1_1159; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_6; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002157; 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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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..375
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000080281"
SQ   SEQUENCE   375 AA;  41202 MW;  22E826CAC4A2E1A7 CRC64;
     MAQLCVALVA GEASGDILGS GLMRALKARH PDVRFIGVGG PLMEAEGLQS YFPMERLAVM
     GLVEVLGRLR ELLKRRKLLI QTLIDEKPDV FIGIDAPDFT LNIELKLRQA GIKTVHYVSP
     SVWAWRQKRV LKIREGCDLM LTLLPFEARF YEEQGVPVRF VGHPLADTIP LEADRSVARA
     ALGLGEGPIV ALMPGSRGGE VGRLGALFLD AAEHLCQQVP GVRFVLPCAN AARRAQVEHM
     LEGRQLPLTL LDGQSHQALA ACDAVLIASG TATLEALLYK RPMVVAYRLA PLTYWILKRL
     VKSPYVSLPN LLAQRELVPE LLQDQATSQA LANTLAPLVR DGSQQTERFD EIHRTLRRDA
     SNQAAEAVLA LLKDR
//