ID   LPXB_HAEDU              Reviewed;         390 AA.
AC   Q7VMW5;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=HD_0846;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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; AE017143; AAP95737.1; -; Genomic_DNA.
DR   RefSeq; WP_010944787.1; NC_002940.2.
DR   AlphaFoldDB; Q7VMW5; -.
DR   SMR; Q7VMW5; -.
DR   STRING; 233412.HD_0846; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; hdu:HD_0846; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OrthoDB; 9801642at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001022; 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   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; Reference proteome; Transferase.
FT   CHAIN           1..390
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190167"
SQ   SEQUENCE   390 AA;  43621 MW;  2052E9E511834324 CRC64;
     MSKDSPLIAL VAGEISGDIL GAGLINALKI HYPNARFIGV AGPQMIQAGC QTLFDMEELA
     VMGLAEVVKH LPRLLKRRKQ VIQTMLQQQP DIFIGIDAPD FNLTIEQKLK AKGITTIHYV
     SPSVWAWRQD RIHKIKRATN LVLAFLPFEK AFYDRFNVAC RFIGHTMADA IALKPNRTEA
     CQILNIDENQ RYLAILAGSR ASEVDFLAEP FLKAALLLKQ KYPDLQCLVP LVNQQRIQQF
     EQIKARVAPS LPVKILKGNA RQAMIAADAT LLASGTAALE AMLCKSPMVV GYKLKPTSYW
     LAKRLIKTKY ISLPNLLADD MLVPELIQDE CNPENLAWYL GNYLADDIDN KKQQNELKQR
     FTDLHKMIQC DADSKAAQAV IDLLANSDDQ
//