(data stored in ACNUC1104 zone)

SWISSPROT: D3UWH2_XENBS

ID   D3UWH2_XENBS            Unreviewed;       389 AA.
AC   D3UWH2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Lipid-A-disaccharide synthase {ECO:0000256|HAMAP-Rule:MF_00392, ECO:0000256|SAAS:SAAS00702238};
DE            EC=2.4.1.182 {ECO:0000256|HAMAP-Rule:MF_00392, ECO:0000256|SAAS:SAAS00702238};
GN   Name=lpxB {ECO:0000256|HAMAP-Rule:MF_00392,
GN   ECO:0000313|EMBL:CBJ79746.1};
GN   OrderedLocusNames=XBJ1_0602 {ECO:0000313|EMBL:CBJ79746.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79746.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79746.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79746.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3-
CC       diacylglucosamine-1-phosphate to form lipid A disaccharide, a
CC       precursor of lipid A, a phosphorylated glycolipid that anchors the
CC       lipopolysaccharide to the outer membrane of the cell.
CC       {ECO:0000256|HAMAP-Rule:MF_00392, ECO:0000256|SAAS:SAAS00702254}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-N,3-O-bis(3-hydroxytetradecanoyl)-alpha-D-glucosaminyl
CC         1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-
CC         alpha-D-glucosamine = H(+) + lipid A disaccharide (E. coli) +
CC         UDP; Xref=Rhea:RHEA:22668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57957,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58466, ChEBI:CHEBI:78847;
CC         EC=2.4.1.182; Evidence={ECO:0000256|HAMAP-Rule:MF_00392,
CC         ECO:0000256|SAAS:SAAS01124936};
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-acetyl-alpha-D-glucosamine: step 5/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00392, ECO:0000256|SAAS:SAAS00702246}.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00392, ECO:0000256|SAAS:SAAS00702241}.
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DR   EMBL; FN667741; CBJ79746.1; -; Genomic_DNA.
DR   STRING; 406818.XBJ1_0602; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; CBJ79746; CBJ79746; XBJ1_0602.
DR   KEGG; xbo:XBJ1_0602; -.
DR   eggNOG; ENOG4105D0V; Bacteria.
DR   eggNOG; COG0763; LUCA.
DR   HOGENOM; HOG000018003; -.
DR   KO; K00748; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00359; UER00481.
DR   Proteomes; UP000002045; 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;
DR   PRODOM; D3UWH2.
DR   SWISS-2DPAGE; D3UWH2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702242, ECO:0000313|EMBL:CBJ79746.1};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702231};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702255};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702243};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702258, ECO:0000313|EMBL:CBJ79746.1}.
SQ   SEQUENCE   389 AA;  42945 MW;  663EF4CBF1E305CB CRC64;
     MATFSSVNNQ RPLTIALVAG ETSGDILGAG LIRALKAQIP DAHFVGVAGP LMQAEGCEAW
     YEMEELAVMG IVEVLGRLPR LLKIRKDLTA RFTALKPDVF VGIDAPDFNI TLEGRLKQRG
     IRTIHYVSPS VWAWRQKRVF KIGRATDLVL AFLPFEKAFY DRFSVPCKFI GHTMADSMPL
     QTDKMAAREA LGVPLNAHCL AILPGSRHAE VEMLSADFLR TVQLLRKILP DLHVLVPLVN
     AKRHQQFQRI KDEIAPDLSV HMLDGNAGKA MIASDATLLA SGTAALECML AKCPMVVGYR
     MKPFTFWLAK RLVKTPYVSL PNLLAGKELV KELLQDECEP QALSEALLPL LQGGADVEAL
     KQTFLHLHES IRCDADEQAA QAVLELARR
//

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