ID   LPXB_PASMU              Reviewed;         392 AA.
AC   Q9CJK7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=PM1997;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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. {ECO:0000250}.
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;
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000305}.
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DR   EMBL; AE004439; AAK04081.1; -; Genomic_DNA.
DR   RefSeq; WP_010907440.1; NC_002663.1.
DR   AlphaFoldDB; Q9CJK7; -.
DR   SMR; Q9CJK7; -.
DR   STRING; 272843.PM1997; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; AAK04081; AAK04081; PM1997.
DR   KEGG; pmu:PM1997; -.
DR   PATRIC; fig|272843.6.peg.2020; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OrthoDB; 9801642at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000809; 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   CDD; cd01635; Glycosyltransferase_GTB-type; 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; Reference proteome; Transferase.
FT   CHAIN           1..392
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190173"
SQ   SEQUENCE   392 AA;  44054 MW;  775F6357A648F910 CRC64;
     MKEIHKQPPT IAIVAGEVSG DILGAGLIRS LKVQYPHARF IGIAGPRMLA EGAETLVDME
     ELSVMGLAEV VKHLPRLLKI RRQLIHTMLQ EKPDIFIGID APDFNIDVEL KLKENGIKTI
     HYVSPSVWAW RQNRIHKIAK ATHLVLAFLP FEKAFYDRFE VPCRFIGHTM ADAIALKPNR
     QEACEYLNLD ASQRYVAILV GSRGSEVTFL AEPFLQAAKL LKQQYPDIQF LVPLINAKRR
     EQFEQIKAQV APELELILLD GKARQAMIAA EATLLASGTA ALEAMLCKSP MVVGYRMKAT
     TYFLAKRLVK TEYVSLPNLL ANEMLVPELI QEQCTAENLA EKLALYLSQE ESALQQRHTL
     IQRFTDLHKL IQCDADKQAA QAVIALLEQE DK
//